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1. Coherent diffractive imaging of microtubules using an X-ray laser.

Author

Brändén, Gisela, Hammarin, Greger, Harimoorthy, Rajiv, Johansson, Alexander, Arnlund, David, Malmerberg, Erik, Barty, Anton, Tångefjord, Stefan, Berntsen, Peter, DePonte, Daniel P, Seuring, Carolin, White, Thomas A, Stellato, Francesco, Bean, Richard, Beyerlein, Kenneth R, Chavas, Leonard MG, Fleckenstein, Holger, Gati, Cornelius, Ghoshdastider, Umesh, Gumprecht, Lars, Oberthür, Dominik, Popp, David, Seibert, Marvin, Tilp, Thomas, Messerschmidt, Marc, Williams, Garth J, Loh, N Duane, Chapman, Henry N, Zwart, Peter, Liang, Mengning, Boutet, Sébastien, Robinson, Robert C, and Neutze, Richard

Subjects
Microtubules, Tubulin, Crystallography, X-Ray, Lasers, Algorithms, Electrons, Synchrotrons, X-Rays, Scattering, Radiation, Image Processing, Computer-Assisted, Molecular Imaging, Crystallography, X-Ray, Scattering, Radiation, Image Processing, Computer-Assisted, Generic Health Relevance, MD Multidisciplinary
Abstract

X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.

Published
2019

3. Ab initio structure determination from experimental fluctuation X-ray scattering data

Author

Pande, Kanupriya, Donatelli, Jeffrey J, Malmerberg, Erik, Foucar, Lutz, Bostedt, Christoph, Schlichting, Ilme, and Zwart, Petrus H

Subjects
Nuclear and Plasma Physics, Physical Sciences, Chlorella, Crystallography, X-Ray, Photoelectron Spectroscopy, Radiography, Research Design, Scattering, Radiation, X-Ray Diffraction, X-Rays, fluctuation X ray scattering, small angle scattering, free electron laser, fluctuation X-ray scattering, free-electron laser, small-angle scattering
Abstract

Fluctuation X-ray scattering (FXS) is an emerging experimental technique in which X-ray solution scattering data are collected from particles in solution using ultrashort X-ray exposures generated by a free-electron laser (FEL). FXS experiments overcome the low data-to-parameter ratios associated with traditional solution scattering measurements by providing several orders of magnitude more information in the final processed data. Here we demonstrate the practical feasibility of FEL-based FXS on a biological multiple-particle system and describe data-processing techniques required to extract robust FXS data and significantly reduce the required number of snapshots needed by introducing an iterative noise-filtering technique. We showcase a successful ab initio electron density reconstruction from such an experiment, studying the Paramecium bursaria Chlorella virus (PBCV-1).

Published
2018

4. Free-electron laser data for multiple-particle fluctuation scattering analysis.

Author

Pande, Kanupriya, Donatelli, Jeffrey J, Malmerberg, Erik, Foucar, Lutz, Poon, Billy K, Sutter, Markus, Botha, Sabine, Basu, Shibom, Bruce Doak, R, Dörner, Katerina, Epp, Sascha W, Englert, Lars, Fromme, Raimund, Hartmann, Elisabeth, Hartmann, Robert, Hauser, Guenter, Hattne, Johan, Hosseinizadeh, Ahmad, Kassemeyer, Stephan, Lomb, Lukas, Montero, Sebastian F Carron, Menzel, Andreas, Rolles, Daniel, Rudenko, Artem, Seibert, Marvin M, Sierra, Raymond George, Schwander, Peter, Ourmazd, Abbas, Fromme, Petra, Sauter, Nicholas K, Bogan, Michael, Bozek, John, Bostedt, Christoph, Schlichting, Ilme, Kerfeld, Cheryl A, and Zwart, Petrus H

Subjects
Phycodnaviridae, X-Ray Diffraction, Scattering, Small Angle
Abstract

Fluctuation X-ray scattering (FXS) is an emerging experimental technique in which solution scattering data are collected using X-ray exposures below rotational diffusion times, resulting in angularly anisotropic X-ray snapshots that provide several orders of magnitude more information than traditional solution scattering data. Such experiments can be performed using the ultrashort X-ray pulses provided by a free-electron laser source, allowing one to collect a large number of diffraction patterns in a relatively short time. Here, we describe a test data set for FXS, obtained at the Linac Coherent Light Source, consisting of close to 100 000 multi-particle diffraction patterns originating from approximately 50 to 200 Paramecium Bursaria Chlorella virus particles per snapshot. In addition to the raw data, a selection of high-quality pre-processed diffraction patterns and a reference SAXS profile are provided.

Published
2018

5. Ultrafast structural changes within a photosynthetic reaction centre

Author

Dods, Robert, Båth, Petra, Morozov, Dmitry, Gagnér, Viktor Ahlberg, Arnlund, David, Luk, Hoi Ling, Kübel, Joachim, Maj, Michał, Vallejos, Adams, Wickstrand, Cecilia, Bosman, Robert, Beyerlein, Kenneth R., Nelson, Garrett, Liang, Mengning, Milathianaki, Despina, Robinson, Joseph, Harimoorthy, Rajiv, Berntsen, Peter, Malmerberg, Erik, Johansson, Linda, Andersson, Rebecka, Carbajo, Sergio, Claesson, Elin, Conrad, Chelsie E., Dahl, Peter, Hammarin, Greger, Hunter, Mark S., Li, Chufeng, Lisova, Stella, Royant, Antoine, Safari, Cecilia, Sharma, Amit, Williams, Garth J., Yefanov, Oleksandr, Westenhoff, Sebastian, Davidsson, Jan, DePonte, Daniel P., Boutet, Sébastien, Barty, Anton, Katona, Gergely, Groenhof, Gerrit, Brändén, Gisela, and Neutze, Richard

Published
2021
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6. Shapes and vorticities of superfluid helium nanodroplets

Author

Gomez, Luis F, Ferguson, Ken R, Cryan, James P, Bacellar, Camila, Tanyag, Rico Mayro P, Jones, Curtis, Schorb, Sebastian, Anielski, Denis, Belkacem, Ali, Bernando, Charles, Boll, Rebecca, Bozek, John, Carron, Sebastian, Chen, Gang, Delmas, Tjark, Englert, Lars, Epp, Sascha W, Erk, Benjamin, Foucar, Lutz, Hartmann, Robert, Hexemer, Alexander, Huth, Martin, Kwok, Justin, Leone, Stephen R, Ma, Jonathan HS, Maia, Filipe RNC, Malmerberg, Erik, Marchesini, Stefano, Neumark, Daniel M, Poon, Billy, Prell, James, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Seifrid, Martin, Siefermann, Katrin R, Sturm, Felix P, Swiggers, Michele, Ullrich, Joachim, Weise, Fabian, Zwart, Petrus, Bostedt, Christoph, Gessner, Oliver, and Vilesov, Andrey F

Subjects
Quantum Physics, Chemical Sciences, Atomic, Molecular and Optical Physics, Physical Sciences, General Science & Technology
Abstract

Helium nanodroplets are considered ideal model systems to explore quantum hydrodynamics in self-contained, isolated superfluids. However, exploring the dynamic properties of individual droplets is experimentally challenging. In this work, we used single-shot femtosecond x-ray coherent diffractive imaging to investigate the rotation of single, isolated superfluid helium-4 droplets containing ~10(8) to 10(11) atoms. The formation of quantum vortex lattices inside the droplets is confirmed by observing characteristic Bragg patterns from xenon clusters trapped in the vortex cores. The vortex densities are up to five orders of magnitude larger than those observed in bulk liquid helium. The droplets exhibit large centrifugal deformations but retain axially symmetric shapes at angular velocities well beyond the stability range of viscous classical droplets.

Published
2014

7. Helium superfluidity. Shapes and vorticities of superfluid helium nanodroplets.

Author

Gomez, Luis F, Ferguson, Ken R, Cryan, James P, Bacellar, Camila, Tanyag, Rico Mayro P, Jones, Curtis, Schorb, Sebastian, Anielski, Denis, Belkacem, Ali, Bernando, Charles, Boll, Rebecca, Bozek, John, Carron, Sebastian, Chen, Gang, Delmas, Tjark, Englert, Lars, Epp, Sascha W, Erk, Benjamin, Foucar, Lutz, Hartmann, Robert, Hexemer, Alexander, Huth, Martin, Kwok, Justin, Leone, Stephen R, Ma, Jonathan HS, Maia, Filipe RNC, Malmerberg, Erik, Marchesini, Stefano, Neumark, Daniel M, Poon, Billy, Prell, James, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Seifrid, Martin, Siefermann, Katrin R, Sturm, Felix P, Swiggers, Michele, Ullrich, Joachim, Weise, Fabian, Zwart, Petrus, Bostedt, Christoph, Gessner, Oliver, and Vilesov, Andrey F

Subjects
General Science & Technology
Abstract

Helium nanodroplets are considered ideal model systems to explore quantum hydrodynamics in self-contained, isolated superfluids. However, exploring the dynamic properties of individual droplets is experimentally challenging. In this work, we used single-shot femtosecond x-ray coherent diffractive imaging to investigate the rotation of single, isolated superfluid helium-4 droplets containing ~10(8) to 10(11) atoms. The formation of quantum vortex lattices inside the droplets is confirmed by observing characteristic Bragg patterns from xenon clusters trapped in the vortex cores. The vortex densities are up to five orders of magnitude larger than those observed in bulk liquid helium. The droplets exhibit large centrifugal deformations but retain axially symmetric shapes at angular velocities well beyond the stability range of viscous classical droplets.

Published
2014

8. Time-resolved protein nanocrystallography using an X-ray free-electron laser

Author

Aquila, Andrew, Hunter, Mark S, Doak, R Bruce, Kirian, Richard A, Fromme, Petra, White, Thomas A, Andreasson, Jakob, Arnlund, David, Bajt, Saša, Barends, Thomas RM, Barthelmess, Miriam, Bogan, Michael J, Bostedt, Christoph, Bottin, Hervé, Bozek, John D, Caleman, Carl, Coppola, Nicola, Davidsson, Jan, DePonte, Daniel P, Elser, Veit, Epp, Sascha W, Erk, Benjamin, Fleckenstein, Holger, Foucar, Lutz, Frank, Matthias, Fromme, Raimund, Graafsma, Heinz, Grotjohann, Ingo, Gumprecht, Lars, Hajdu, Janos, Hampton, Christina Y, Hartmann, Andreas, Hartmann, Robert, Hau-Riege, Stefan, Hauser, Günter, Hirsemann, Helmut, Holl, Peter, Holton, James M, Hömke, André, Johansson, Linda, Kimmel, Nils, Kassemeyer, Stephan, Krasniqi, Faton, Kühnel, Kai-Uwe, Liang, Mengning, Lomb, Lukas, Malmerberg, Erik, Marchesini, Stefano, Martin, Andrew V, Maia, Filipe RNC, Messerschmidt, Marc, Nass, Karol, Reich, Christian, Neutze, Richard, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Schlichting, Ilme, Schmidt, Carlo, Schmidt, Kevin E, Schulz, Joachim, Seibert, M Marvin, Shoeman, Robert L, Sierra, Raymond, Soltau, Heike, Starodub, Dmitri, Stellato, Francesco, Stern, Stephan, Strüder, Lothar, Timneanu, Nicusor, Ullrich, Joachim, Wang, Xiaoyu, Williams, Garth J, Weidenspointner, Georg, Weierstall, Uwe, Wunderer, Cornelia, Barty, Anton, Spence, John CH, and Chapman, Henry N

Subjects
Crystallography, X-Ray, Electrons, Ferredoxins, Lasers, Nanostructures, Protein Conformation, X-Ray Diffraction, X-Rays, Optical Physics, Electrical and Electronic Engineering, Communications Technologies, Optics
Abstract

We demonstrate the use of an X-ray free electron laser synchronized with an optical pump laser to obtain X-ray diffraction snapshots from the photoactivated states of large membrane protein complexes in the form of nanocrystals flowing in a liquid jet. Light-induced changes of Photosystem I-Ferredoxin co-crystals were observed at time delays of 5 to 10 µs after excitation. The result correlates with the microsecond kinetics of electron transfer from Photosystem I to ferredoxin. The undocking process that follows the electron transfer leads to large rearrangements in the crystals that will terminally lead to the disintegration of the crystals. We describe the experimental setup and obtain the first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source. This technique opens the door to time-resolved structural studies of reaction dynamics in biological systems.

Published
2012

9. From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography

Author

Dods, Robert, Båth, Petra, Arnlund, David, Beyerlein, Kenneth R., Nelson, Garrett, Liang, Mengling, Harimoorthy, Rajiv, Berntsen, Peter, Malmerberg, Erik, Johansson, Linda, Andersson, Rebecka, Bosman, Robert, Carbajo, Sergio, Claesson, Elin, Conrad, Chelsie E., Dahl, Peter, Hammarin, Greger, Hunter, Mark S., Li, Chufeng, Lisova, Stella, Milathianaki, Despina, Robinson, Joseph, Safari, Cecilia, Sharma, Amit, Williams, Garth, Wickstrand, Cecilia, Yefanov, Oleksandr, Davidsson, Jan, DePonte, Daniel P., Barty, Anton, Brändén, Gisela, and Neutze, Richard

Published
2017
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10. Author Correction: Coherent diffractive imaging of microtubules using an X-ray laser

Author

Brändén, Gisela, Hammarin, Greger, Harimoorthy, Rajiv, Johansson, Alexander, Arnlund, David, Malmerberg, Erik, Barty, Anton, Tångefjord, Stefan, Berntsen, Peter, DePonte, Daniel P., Seuring, Carolin, White, Thomas A., Stellato, Francesco, Bean, Richard, Beyerlein, Kenneth R., Chavas, Leonard M. G., Fleckenstein, Holger, Gati, Cornelius, Ghoshdastider, Umesh, Gumprecht, Lars, Oberthür, Dominik, Popp, David, Seibert, Marvin, Tilp, Thomas, Messerschmidt, Marc, Williams, Garth J., Loh, N. Duane, Chapman, Henry N., Zwart, Peter, Liang, Mengning, Boutet, Sébastien, Robinson, Robert C., and Neutze, Richard

Published
2019
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13. Structural Dynamics of Light-Driven Proton Pumps

Author

Andersson, Magnus, Malmerberg, Erik, Westenhoff, Sebastian, Katona, Gergely, Cammarata, Marco, Wöhri, Annemarie B., Johansson, Linda C., Ewald, Friederike, Eklund, Mattias, Wulff, Michael, Davidsson, Jan, and Neutze, Richard

Published
2009
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15. Ultrafast structural changes within a photosynthetic reaction centre

Author

Dods, Robert, primary, Båth, Petra, additional, Morozov, Dmitry, additional, Gagnér, Viktor Ahlberg, additional, Arnlund, David, additional, Luk, Hoi Ling, additional, Kübel, Joachim, additional, Maj, Michał, additional, Vallejos, Adams, additional, Wickstrand, Cecilia, additional, Bosman, Robert, additional, Beyerlein, Kenneth R., additional, Nelson, Garrett, additional, Liang, Mengning, additional, Milathianaki, Despina, additional, Robinson, Joseph, additional, Harimoorthy, Rajiv, additional, Berntsen, Peter, additional, Malmerberg, Erik, additional, Johansson, Linda, additional, Andersson, Rebecka, additional, Carbajo, Sergio, additional, Claesson, Elin, additional, Conrad, Chelsie E., additional, Dahl, Peter, additional, Hammarin, Greger, additional, Hunter, Mark S., additional, Li, Chufeng, additional, Lisova, Stella, additional, Royant, Antoine, additional, Safari, Cecilia, additional, Sharma, Amit, additional, Williams, Garth J., additional, Yefanov, Oleksandr, additional, Westenhoff, Sebastian, additional, Davidsson, Jan, additional, DePonte, Daniel P., additional, Boutet, Sébastien, additional, Barty, Anton, additional, Katona, Gergely, additional, Groenhof, Gerrit, additional, Brändén, Gisela, additional, and Neutze, Richard, additional

Published
2020
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18. Transient isomers in the photodissociation of bromoiodomethane

Author

Marcellini, Moreno, primary, Nasedkin, Alexandr, additional, Zietz, Burkhard, additional, Petersson, Jonas, additional, Vincent, Jonathan, additional, Palazzetti, Federico, additional, Malmerberg, Erik, additional, Kong, Qingyu, additional, Wulff, Michael, additional, van der Spoel, David, additional, Neutze, Richard, additional, and Davidsson, Jan, additional

Published
2018
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19. Solvent dependent structural perturbations of chemical reaction intermediates visualized by time-resolved x-ray diffraction.

Author

Vincent, Jonathan, Andersson, Magnus, Eklund, Mattias, Wöhri, Annemarie B., Odelius, Michael, Malmerberg, Erik, Kong, Qingyu, Wulff, Michael, Neutze, Richard, and Davidsson, Jan

Subjects
X-ray scattering, CYCLOHEXANE, CHEMICAL reactions, X-ray diffraction, METHANOL, THERMODYNAMICS, QUANTUM theory, PHYSICAL & theoretical chemistry
Abstract

Ultrafast time-resolved wide angle x-ray scattering from chemical reactions in solution has recently emerged as a powerful technique for determining the structural dynamics of transient photochemical species. Here we examine the structural evolution of photoexcited CH2I2 in the nonpolar solvent cyclohexane and draw comparisons with a similar study in the polar solvent methanol. As with earlier spectroscopic studies, our data confirm a common initial reaction pathway in both solvents. After photoexcitation, CH2I2 dissociates to form CH2I·+I·. Iodine radicals remaining within the solvent cage recombine with a nascent CH2I· radical to form the transient isomer CH2I-I, whereas those which escape the solvent cage ultimately combine to form I2 in cyclohexane. Moreover, the transient isomer has a lifetime approximately 30 times longer in the nonpolar solvent. Of greater chemical significance is the property of time-resolved wide angle x-ray diffraction to accurately determine the structure of the of CH2I-I reaction intermediate. Thus we observe that the transient iodine-iodine bond is 0.07 ű0.04 Å shorter in cyclohexane than in methanol. A longer iodine-iodine bond length for the intermediate arises in methanol due to favorable H-bond interaction with the polar solvent. These findings establish that time-resolved x-ray diffraction has sufficient sensitivity to enable solvent dependent structural perturbations of transient chemical species to be accurately resolved. [ABSTRACT FROM AUTHOR]

Published
2009
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20. Transient isomers in the photodissociation of bromoiodomethane

Author

Marcellini, Moreno, Nasedkin, Alexandr, Zietz, Burkhard, Petersson, Jonas, Vincent, Jonathan, Palazzetti, Federico, Malmerberg, Erik, Kong, Qingyu, Wulff, Michael, van der Spoel, David, Neutze, Richard, Davidsson, Jan, Marcellini, Moreno, Nasedkin, Alexandr, Zietz, Burkhard, Petersson, Jonas, Vincent, Jonathan, Palazzetti, Federico, Malmerberg, Erik, Kong, Qingyu, Wulff, Michael, van der Spoel, David, Neutze, Richard, and Davidsson, Jan

Abstract

The photochemistry of halomethanes is fascinating for the complex cascade reactions toward either the parent or newly synthesized molecules. Here, we address the structural rearrangement of photodissociated CH2IBr in methanol and cyclohexane, probed by time-resolved X-ray scattering in liquid solution. Upon selective laser cleavage of the C-I bond, we follow the reaction cascade of the two geminate geometrical isomers, CH2I-Br and CH2Br-I. Both meta-stable isomers decay on different time scales, mediated by solvent interaction, toward the original parent molecule. We observe the internal rearrangement of CH2Br-I to CH2I-Br in cyclohexane by extending the time window up to 3 mu s. We track the photoproduct kinetics of CH2Br-I in methanol solution where only one isomer is observed. The effect of the polarity of solvent on the geminate recombination pathways is discussed.

Published
2018
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21. Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface

Author

Wohri, Annemarie B., Wahlgren, Weixiao Y., Malmerberg, Erik, Johansson, Linda C., Neutze, Richard, and Katona, Gergely

Subjects
Blastochloris viridis -- Research, Photosynthesis -- Analysis, Ubiquinones -- Chemical properties, Ubiquinones -- Structure, Electrons -- Diffraction, Electrons -- Usage, Biological sciences, Chemistry
Abstract

The lipidic sponge phase crystal structure of the reaction center from Blastochloris viridis to 1.86 [Angstrom] which revealed lipid molecules interacting with the protein surface is presented. The electron density data recovered at the [Q.sub.B] site and the observed change in recombination kinetics in lipidic sponge phase-grown crystals suggested that the mobile ubiquinone appeared to be displaced by a monoolein molecule.

Published
2009

22. Conformational Dynamics of Rhodopsins Visualized by Time-resolved Wide Angle X-ray Scattering

Author

Malmerberg, Erik

Subjects
Rhodopsin, Proteorhodopsin, Retinylidene proteins, Bacteriorhodopsin, Time-resolved wide Angle X-ray Scattering
Abstract

Rhodopsins are a family of light-sensitive proteins found in the cellular membranes of a wide range of living organisms. These membrane proteins share a common molecular architecture and are able to use light energy to perform a variety of different biological functions. Mapping the conformational changes required for these proteins to function is important for understanding how light energy is used for energy transduction and sensory perception in biological systems. In order to visualize these conformational changes over time, the emerging technique of time-resolved wide angle X-ray scattering (TR-WAXS) was employed. Several technical and analytical developments of this solution based method were made during the course of this work, including the development of a new data collection strategy based on a rapid readout X-ray detector. The light-driven proton pumps bacteriorhodopsin and proteorhodopsin were the first membrane proteins to be characterized using TR-WAXS. The results from these studies indicated that significant α-helical rearrangements precede the primary proton transfer event in bacteriorhodopsin. Comparison with the evolutionary related proteorhodopsin provided important insights into shared conformational dynamics between the two proton-pumps. Proteorhodopsin was further investigated by probing the conformational changes occurring within its chromophore binding pocket, where the chromophore of proteorhodopsin was substituted with a chemically modified retinal analogue. Comparison between the native and modified form of proteorhodopsin indicated significant chromophore dependant differences in their conformational kinetics. These differences provided new insights into the coupling between retinal isomerisation and protein conformational changes. The conformational dynamics within visual rhodopsin, the primary light sensor of vertebrate vision, were also investigated using TR-WAXS. By using the rapid readout X-ray detector we were able to follow the activation of this G-protein coupled receptor in real-time. Structural analysis further indicated that dramatic conformational changes are associated with the activation of this receptor.

Published
2011

24. Conformational activation of visual rhodopsin in native disc membranes

Author

Malmerberg, Erik, primary, M. Bovee-Geurts, Petra H., additional, Katona, Gergely, additional, Deupi, Xavier, additional, Arnlund, David, additional, Wickstrand, Cecilia, additional, Johansson, Linda C., additional, Westenhoff, Sebastian, additional, Nazarenko, Elena, additional, X. Schertler, Gebhard F., additional, Menzel, Andreas, additional, de Grip, Willem J., additional, and Neutze, Richard, additional

Published
2015
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25. Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser

Author

Arnlund, David, Johansson, Linda C, Wickstrand, Cecilia, Barty, Anton, Williams, Garth J, Malmerberg, Erik, Davidsson, Jan, Milathianaki, Despina, DePonte, Daniel P, Shoeman, Robert L, Wang, Dingjie, James, Daniel, Katona, Gergely, Westenhoff, Sebastian, White, Thomas A, Aquila, Andrew, Bari, Sadia, Berntsen, Peter, Bogan, Mike, van Driel, Tim Brandt, Doak, R Bruce, Kjær, Kasper Skov, Frank, Matthias, Fromme, Raimund, Grotjohann, Ingo, Henning, Robert, Hunter, Mark S, Kirian, Richard A, Kosheleva, Irina, Kupitz, Christopher, Liang, Mengning, Martin, Andrew V, Nielsen, Martin Meedom, Messerschmidt, Marc, Seibert, M Marvin, Sjöhamn, Jennie, Stellato, Francesco, Weierstall, Uwe, Zatsepin, Nadia A, Spence, John C H, Fromme, Petra, Schlichting, Ilme, Boutet, Sébastien, Groenhof, Gerrit, Chapman, Henry N, Neutze, Richard, Arnlund, David, Johansson, Linda C, Wickstrand, Cecilia, Barty, Anton, Williams, Garth J, Malmerberg, Erik, Davidsson, Jan, Milathianaki, Despina, DePonte, Daniel P, Shoeman, Robert L, Wang, Dingjie, James, Daniel, Katona, Gergely, Westenhoff, Sebastian, White, Thomas A, Aquila, Andrew, Bari, Sadia, Berntsen, Peter, Bogan, Mike, van Driel, Tim Brandt, Doak, R Bruce, Kjær, Kasper Skov, Frank, Matthias, Fromme, Raimund, Grotjohann, Ingo, Henning, Robert, Hunter, Mark S, Kirian, Richard A, Kosheleva, Irina, Kupitz, Christopher, Liang, Mengning, Martin, Andrew V, Nielsen, Martin Meedom, Messerschmidt, Marc, Seibert, M Marvin, Sjöhamn, Jennie, Stellato, Francesco, Weierstall, Uwe, Zatsepin, Nadia A, Spence, John C H, Fromme, Petra, Schlichting, Ilme, Boutet, Sébastien, Groenhof, Gerrit, Chapman, Henry N, and Neutze, Richard

Abstract

We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.

Published
2014
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26. Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser

Author

Arnlund, David, primary, Johansson, Linda C, additional, Wickstrand, Cecilia, additional, Barty, Anton, additional, Williams, Garth J, additional, Malmerberg, Erik, additional, Davidsson, Jan, additional, Milathianaki, Despina, additional, DePonte, Daniel P, additional, Shoeman, Robert L, additional, Wang, Dingjie, additional, James, Daniel, additional, Katona, Gergely, additional, Westenhoff, Sebastian, additional, White, Thomas A, additional, Aquila, Andrew, additional, Bari, Sadia, additional, Berntsen, Peter, additional, Bogan, Mike, additional, van Driel, Tim Brandt, additional, Doak, R Bruce, additional, Kjær, Kasper Skov, additional, Frank, Matthias, additional, Fromme, Raimund, additional, Grotjohann, Ingo, additional, Henning, Robert, additional, Hunter, Mark S, additional, Kirian, Richard A, additional, Kosheleva, Irina, additional, Kupitz, Christopher, additional, Liang, Mengning, additional, Martin, Andrew V, additional, Nielsen, Martin Meedom, additional, Messerschmidt, Marc, additional, Seibert, M Marvin, additional, Sjöhamn, Jennie, additional, Stellato, Francesco, additional, Weierstall, Uwe, additional, Zatsepin, Nadia A, additional, Spence, John C H, additional, Fromme, Petra, additional, Schlichting, Ilme, additional, Boutet, Sébastien, additional, Groenhof, Gerrit, additional, Chapman, Henry N, additional, and Neutze, Richard, additional

Published
2014
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27. Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography

Author

Johansson, Linda C., Arnlund, David, Katona, Gergely, White, Thomas A., Barty, Anton, DePonte, Daniel P., Shoeman, Robert L., Wickstrand, Cecilia, Sharma, Amit, Williams, Garth J., Aquila, Andrew, Bogan, Michael J., Caleman, Carl, Davidsson, Jan, Doak, R. Bruce, Frank, Matthias, Fromme, Raimund, Galli, Lorenzo, Grotjohann, Ingo, Hunter, Mark S., Kassemeyer, Stephan, Kirian, Richard A., Kupitz, Christopher, Liang, Mengning, Lomb, Lukas, Malmerberg, Erik, Martin, Andrew V., Messerschmidt, Marc, Nass, Karol, Redecke, Lars, Seibert, M. Marvin, Sjoehamn, Jennie, Steinbrener, Jan, Stellato, Francesco, Wang, Dingjie, Wahlgren, Weixaio Y., Weierstall, Uwe, Westenhoff, Sebastian, Zatsepin, Nadia A., Boutet, Sebastien, Spence, John C. H., Schlichting, Ilme, Chapman, Henry N., Fromme, Petra, Neutze, Richard, Johansson, Linda C., Arnlund, David, Katona, Gergely, White, Thomas A., Barty, Anton, DePonte, Daniel P., Shoeman, Robert L., Wickstrand, Cecilia, Sharma, Amit, Williams, Garth J., Aquila, Andrew, Bogan, Michael J., Caleman, Carl, Davidsson, Jan, Doak, R. Bruce, Frank, Matthias, Fromme, Raimund, Galli, Lorenzo, Grotjohann, Ingo, Hunter, Mark S., Kassemeyer, Stephan, Kirian, Richard A., Kupitz, Christopher, Liang, Mengning, Lomb, Lukas, Malmerberg, Erik, Martin, Andrew V., Messerschmidt, Marc, Nass, Karol, Redecke, Lars, Seibert, M. Marvin, Sjoehamn, Jennie, Steinbrener, Jan, Stellato, Francesco, Wang, Dingjie, Wahlgren, Weixaio Y., Weierstall, Uwe, Westenhoff, Sebastian, Zatsepin, Nadia A., Boutet, Sebastien, Spence, John C. H., Schlichting, Ilme, Chapman, Henry N., Fromme, Petra, and Neutze, Richard

Abstract

Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 angstrom resolution and determine its serial femtosecond crystallography structure to 3.5 angstrom resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

Published
2013
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28. Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements

Author

Barty, Anton, Caleman, Carl, Aquila, Andrew, Timneanu, Nicusor, Lomb, Lukas, White, Thomas A., Andreasson, Jakob, Arnlund, David, Bajt, Sasa, Barends, Thomas R. M., Barthelmess, Miriam, Bogan, Michael J., Bostedt, Christoph, Bozek, John D., Coffee, Ryan, Coppola, Nicola, Davidsson, Jan, DePonte, Daniel P., Doak, R. Bruce, Ekeberg, Tomas, Elser, Veit, Epp, Sascha W., Erk, Benjamin, Fleckenstein, Holger, Foucar, Lutz, Fromme, Petra, Graafsma, Heinz, Gumprecht, Lars, Hajdu, Janos, Hampton, Christina Y., Hartmann, Robert, Hartmann, Andreas, Hauser, Guenter, Hirsemann, Helmut, Holl, Peter, Hunter, Mark S., Johansson, Linda, Kassemeyer, Stephan, Kimmel, Nils, Kirian, Richard A., Liang, Mengning, Maia, Filipe R. N. C., Malmerberg, Erik, Marchesini, Stefano, Martin, Andrew V., Nass, Karol, Neutze, Richard, Reich, Christian, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Scott, Howard, Schlichting, Ilme, Schulz, Joachim, Seibert, M. Marvin, Shoeman, Robert L., Sierra, Raymond G., Soltau, Heike, Spence, John C. H., Stellato, Francesco, Stern, Stephan, Strueder, Lothar, Ullrich, Joachim, Wang, X., Weidenspointner, Georg, Weierstall, Uwe, Wunderer, Cornelia B., Chapman, Henry N., Barty, Anton, Caleman, Carl, Aquila, Andrew, Timneanu, Nicusor, Lomb, Lukas, White, Thomas A., Andreasson, Jakob, Arnlund, David, Bajt, Sasa, Barends, Thomas R. M., Barthelmess, Miriam, Bogan, Michael J., Bostedt, Christoph, Bozek, John D., Coffee, Ryan, Coppola, Nicola, Davidsson, Jan, DePonte, Daniel P., Doak, R. Bruce, Ekeberg, Tomas, Elser, Veit, Epp, Sascha W., Erk, Benjamin, Fleckenstein, Holger, Foucar, Lutz, Fromme, Petra, Graafsma, Heinz, Gumprecht, Lars, Hajdu, Janos, Hampton, Christina Y., Hartmann, Robert, Hartmann, Andreas, Hauser, Guenter, Hirsemann, Helmut, Holl, Peter, Hunter, Mark S., Johansson, Linda, Kassemeyer, Stephan, Kimmel, Nils, Kirian, Richard A., Liang, Mengning, Maia, Filipe R. N. C., Malmerberg, Erik, Marchesini, Stefano, Martin, Andrew V., Nass, Karol, Neutze, Richard, Reich, Christian, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Scott, Howard, Schlichting, Ilme, Schulz, Joachim, Seibert, M. Marvin, Shoeman, Robert L., Sierra, Raymond G., Soltau, Heike, Spence, John C. H., Stellato, Francesco, Stern, Stephan, Strueder, Lothar, Ullrich, Joachim, Wang, X., Weidenspointner, Georg, Weierstall, Uwe, Wunderer, Cornelia B., and Chapman, Henry N.

Abstract

X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis(1). For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information(1-4). Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology(5) should enable structural determination from submicrometre protein crystals with atomic resolution.

Published
2012
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29. Lipidic phase membrane protein serial femtosecond crystallography

Author

Johansson, Linda C, Arnlund, David, White, Thomas A, Katona, Gergely, DePonte, Daniel P, Weierstall, Uwe, Doak, R Bruce, Shoeman, Robert L, Lomb, Lukas, Malmerberg, Erik, Davidsson, Jan, Nass, Karol, Liang, Mengning, Andreasson, Jakob, Aquila, Andrew, Bajt, Sasa, Barthelmess, Miriam, Barty, Anton, Bogan, Michael J, Bostedt, Christoph, Bozek, John D, Caleman, Carl, Coffee, Ryan, Coppola, Nicola, Ekeberg, Tomas, Epp, Sascha W, Erk, Benjamin, Fleckenstein, Holger, Foucar, Lutz, Graafsma, Heinz, Gumprecht, Lars, Hajdu, Janos, Hampton, Christina Y, Hartmann, Robert, Hartmann, Andreas, Hauser, Gunter, Hirsemann, Helmut, Holl, Peter, Hunter, Mark S, Kassemeyer, Stephan, Kimmel, Nils, Kirian, Richard A, Maia, Filipe R N C, Marchesini, Stefano, Martin, Andrew V, Reich, Christian, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Schlichting, Ilme, Schulz, Joachim, Seibert, M Marvin, Sierra, Raymond G, Soltau, Heike, Starodub, Dmitri, Stellato, Francesco, Stern, Stephan, Struder, Lothar, Timneanu, Nicusor, Ullrich, Joachim, Wahlgren, Weixiao Y, Wang, Xiaoyu, Weidenspointner, Georg, Wunderer, Cornelia, Fromme, Petra, Chapman, Henry N, Spence, John C H, Neutze, Richard, Johansson, Linda C, Arnlund, David, White, Thomas A, Katona, Gergely, DePonte, Daniel P, Weierstall, Uwe, Doak, R Bruce, Shoeman, Robert L, Lomb, Lukas, Malmerberg, Erik, Davidsson, Jan, Nass, Karol, Liang, Mengning, Andreasson, Jakob, Aquila, Andrew, Bajt, Sasa, Barthelmess, Miriam, Barty, Anton, Bogan, Michael J, Bostedt, Christoph, Bozek, John D, Caleman, Carl, Coffee, Ryan, Coppola, Nicola, Ekeberg, Tomas, Epp, Sascha W, Erk, Benjamin, Fleckenstein, Holger, Foucar, Lutz, Graafsma, Heinz, Gumprecht, Lars, Hajdu, Janos, Hampton, Christina Y, Hartmann, Robert, Hartmann, Andreas, Hauser, Gunter, Hirsemann, Helmut, Holl, Peter, Hunter, Mark S, Kassemeyer, Stephan, Kimmel, Nils, Kirian, Richard A, Maia, Filipe R N C, Marchesini, Stefano, Martin, Andrew V, Reich, Christian, Rolles, Daniel, Rudek, Benedikt, Rudenko, Artem, Schlichting, Ilme, Schulz, Joachim, Seibert, M Marvin, Sierra, Raymond G, Soltau, Heike, Starodub, Dmitri, Stellato, Francesco, Stern, Stephan, Struder, Lothar, Timneanu, Nicusor, Ullrich, Joachim, Wahlgren, Weixiao Y, Wang, Xiaoyu, Weidenspointner, Georg, Wunderer, Cornelia, Fromme, Petra, Chapman, Henry N, Spence, John C H, and Neutze, Richard

Abstract

X-ray free electron laser (X-FEL)-based serial femtosecond crystallography is an emerging method with potential to rapidly advance the challenging field of membrane protein structural biology. Here we recorded interpretable diffraction data from micrometer-sized lipidic sponge phase crystals of the Blastochloris viridis photosynthetic reaction center delivered into an X-FEL beam using a sponge phase micro-jet.

Published
2012
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30. Rapid readout detector captures protein time-resolved WAXS

Author

Westenhoff, Sebastian, Malmerberg, Erik, Arnlund, David, Johansson, Linda, Nazarenko, Elena, Cammarata, Marco, Davidsson, Jan, Chaptal, Vincent, Abramson, Jeff, Katona, Gergely, Menzel, Andreas, Neutze, Richard, Westenhoff, Sebastian, Malmerberg, Erik, Arnlund, David, Johansson, Linda, Nazarenko, Elena, Cammarata, Marco, Davidsson, Jan, Chaptal, Vincent, Abramson, Jeff, Katona, Gergely, Menzel, Andreas, and Neutze, Richard

Published
2010
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31. Time-resolved structural studies of protein reaction dynamics : a smorgasbord of X-ray approaches

Author

Westenhoff, Sebastian, Nazarenko, Elena, Malmerberg, Erik, Davidsson, Jan, Katona, Gergely, Neutze, Richard, Westenhoff, Sebastian, Nazarenko, Elena, Malmerberg, Erik, Davidsson, Jan, Katona, Gergely, and Neutze, Richard

Abstract

Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein's resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein's conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein's reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and time-resolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics. These methods are illustrated using a limited set of examples including myoglobin and haemoglobin in complex with carbon monoxide, the simple light-driven proton pump bacteriorhodopsin, and the superoxide scavenger superoxide reductase. In conclusion, likely future developments of these methods at synchrotron X-ray sources and the potential impact of emerging X-ray free-electron laser facilities are speculated upon.

Published
2010
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32. Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography

Author

Johansson, Linda C., primary, Arnlund, David, additional, Katona, Gergely, additional, White, Thomas A., additional, Barty, Anton, additional, DePonte, Daniel P., additional, Shoeman, Robert L., additional, Wickstrand, Cecilia, additional, Sharma, Amit, additional, Williams, Garth J., additional, Aquila, Andrew, additional, Bogan, Michael J., additional, Caleman, Carl, additional, Davidsson, Jan, additional, Doak, R Bruce, additional, Frank, Matthias, additional, Fromme, Raimund, additional, Galli, Lorenzo, additional, Grotjohann, Ingo, additional, Hunter, Mark S., additional, Kassemeyer, Stephan, additional, Kirian, Richard A., additional, Kupitz, Christopher, additional, Liang, Mengning, additional, Lomb, Lukas, additional, Malmerberg, Erik, additional, Martin, Andrew V., additional, Messerschmidt, Marc, additional, Nass, Karol, additional, Redecke, Lars, additional, Seibert, M Marvin, additional, Sjöhamn, Jennie, additional, Steinbrener, Jan, additional, Stellato, Francesco, additional, Wang, Dingjie, additional, Wahlgren, Weixaio Y., additional, Weierstall, Uwe, additional, Westenhoff, Sebastian, additional, Zatsepin, Nadia A., additional, Boutet, Sébastien, additional, Spence, John C.H., additional, Schlichting, Ilme, additional, Chapman, Henry N., additional, Fromme, Petra, additional, and Neutze, Richard, additional

Published
2013
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33. Lipidic phase membrane protein serial femtosecond crystallography

Author

Johansson, Linda C, primary, Arnlund, David, additional, White, Thomas A, additional, Katona, Gergely, additional, DePonte, Daniel P, additional, Weierstall, Uwe, additional, Doak, R Bruce, additional, Shoeman, Robert L, additional, Lomb, Lukas, additional, Malmerberg, Erik, additional, Davidsson, Jan, additional, Nass, Karol, additional, Liang, Mengning, additional, Andreasson, Jakob, additional, Aquila, Andrew, additional, Bajt, Saša, additional, Barthelmess, Miriam, additional, Barty, Anton, additional, Bogan, Michael J, additional, Bostedt, Christoph, additional, Bozek, John D, additional, Caleman, Carl, additional, Coffee, Ryan, additional, Coppola, Nicola, additional, Ekeberg, Tomas, additional, Epp, Sascha W, additional, Erk, Benjamin, additional, Fleckenstein, Holger, additional, Foucar, Lutz, additional, Graafsma, Heinz, additional, Gumprecht, Lars, additional, Hajdu, Janos, additional, Hampton, Christina Y, additional, Hartmann, Robert, additional, Hartmann, Andreas, additional, Hauser, Günter, additional, Hirsemann, Helmut, additional, Holl, Peter, additional, Hunter, Mark S, additional, Kassemeyer, Stephan, additional, Kimmel, Nils, additional, Kirian, Richard A, additional, Maia, Filipe R N C, additional, Marchesini, Stefano, additional, Martin, Andrew V, additional, Reich, Christian, additional, Rolles, Daniel, additional, Rudek, Benedikt, additional, Rudenko, Artem, additional, Schlichting, Ilme, additional, Schulz, Joachim, additional, Seibert, M Marvin, additional, Sierra, Raymond G, additional, Soltau, Heike, additional, Starodub, Dmitri, additional, Stellato, Francesco, additional, Stern, Stephan, additional, Strüder, Lothar, additional, Timneanu, Nicusor, additional, Ullrich, Joachim, additional, Wahlgren, Weixiao Y, additional, Wang, Xiaoyu, additional, Weidenspointner, Georg, additional, Wunderer, Cornelia, additional, Fromme, Petra, additional, Chapman, Henry N, additional, Spence, John C H, additional, and Neutze, Richard, additional

Published
2012
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34. Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements

Author

Barty, Anton, primary, Caleman, Carl, additional, Aquila, Andrew, additional, Timneanu, Nicusor, additional, Lomb, Lukas, additional, White, Thomas A., additional, Andreasson, Jakob, additional, Arnlund, David, additional, Bajt, Saša, additional, Barends, Thomas R. M., additional, Barthelmess, Miriam, additional, Bogan, Michael J., additional, Bostedt, Christoph, additional, Bozek, John D., additional, Coffee, Ryan, additional, Coppola, Nicola, additional, Davidsson, Jan, additional, DePonte, Daniel P., additional, Doak, R. Bruce, additional, Ekeberg, Tomas, additional, Elser, Veit, additional, Epp, Sascha W., additional, Erk, Benjamin, additional, Fleckenstein, Holger, additional, Foucar, Lutz, additional, Fromme, Petra, additional, Graafsma, Heinz, additional, Gumprecht, Lars, additional, Hajdu, Janos, additional, Hampton, Christina Y., additional, Hartmann, Robert, additional, Hartmann, Andreas, additional, Hauser, Günter, additional, Hirsemann, Helmut, additional, Holl, Peter, additional, Hunter, Mark S., additional, Johansson, Linda, additional, Kassemeyer, Stephan, additional, Kimmel, Nils, additional, Kirian, Richard A., additional, Liang, Mengning, additional, Maia, Filipe R. N. C., additional, Malmerberg, Erik, additional, Marchesini, Stefano, additional, Martin, Andrew V., additional, Nass, Karol, additional, Neutze, Richard, additional, Reich, Christian, additional, Rolles, Daniel, additional, Rudek, Benedikt, additional, Rudenko, Artem, additional, Scott, Howard, additional, Schlichting, Ilme, additional, Schulz, Joachim, additional, Seibert, M. Marvin, additional, Shoeman, Robert L., additional, Sierra, Raymond G., additional, Soltau, Heike, additional, Spence, John C. H., additional, Stellato, Francesco, additional, Stern, Stephan, additional, Strüder, Lothar, additional, Ullrich, Joachim, additional, Wang, X., additional, Weidenspointner, Georg, additional, Weierstall, Uwe, additional, Wunderer, Cornelia B., additional, and Chapman, Henry N., additional

Published
2011
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36. Rapid readout detector captures protein time-resolved WAXS

Author

Westenhoff, Sebastian, primary, Malmerberg, Erik, additional, Arnlund, David, additional, Johansson, Linda, additional, Nazarenko, Elena, additional, Cammarata, Marco, additional, Davidsson, Jan, additional, Chaptal, Vincent, additional, Abramson, Jeff, additional, Katona, Gergely, additional, Menzel, Andreas, additional, and Neutze, Richard, additional

Published
2010
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37. Light-induced structural changes in photosynthetic reaction centres

Author

Katona, Gergely, primary, Wöhri, Annemarie, additional, Johansson, Linda C., additional, Fritz, Emelie, additional, Malmerberg, Erik, additional, Andersson, Magnus, additional, Vincent, Jonathan, additional, Eklund, Mattias, additional, Cammarata, Marco, additional, Wulff, Michael, additional, Davidsson, Jan, additional, Groenhof, Gerrit, additional, and Neutze, Richard, additional

Published
2010
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38. Lipidic sponge phase crystallization of photosynthetic reaction centres

Author

Katona, Gergely, primary, Wöhri, Annemarie, additional, Wahlgren, Weixiao Y., additional, Johansson, Linda C., additional, Fritz, Emelie, additional, Malmerberg, Erik, additional, Andersson, Magnus, additional, Vincent, Jonathan, additional, Eklund, Mattias, additional, Cammarata, Marco, additional, Wulff, Michael, additional, Davidsson, Jan, additional, Groenhof, Gerrit, additional, and Neutze, Richard, additional

Published
2010
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40. Structural Dynamics of Light-Driven Proton Pumps

Author

Andersson, Magnus, primary, Malmerberg, Erik, additional, Westenhoff, Sebastian, additional, Katona, Gergely, additional, Cammarata, Marco, additional, Wohri, Annemarie B., additional, Johansson, Linda C., additional, Ewald, Friederike, additional, Eklund, Mattias, additional, Wulff, Michael, additional, Davidsson, Jan, additional, and Neutze, Richard, additional

Published
2010
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41. Coherent diffractive imaging of microtubules using an X-ray laser

Author

Brändén, Gisela, Hammarin, Greger, Harimoorthy, Rajiv, Johansson, Alexander, Arnlund, David, Malmerberg, Erik, Barty, Anton, Tångefjord, Stefan, Berntsen, Peter, DePonte, Daniel P., Seuring, Carolin, White, Thomas A., Stellato, Francesco, Bean, Richard, Beyerlein, Kenneth R., Chavas, Leonard M. G., Fleckenstein, Holger, Gati, Cornelius, Ghoshdastider, Umesh, Gumprecht, Lars, Oberthür, Dominik, Popp, David, Seibert, Marvin, Tilp, Thomas, Messerschmidt, Marc, Williams, Garth, Loh, N. Duane, Chapman, Henry N., Zwart, Peter, Liang, Mengning, Boutet, Sébastien, Robinson, Robert C., and Neutze, Richard

Subjects
3. Good health
Abstract

Nature Communications 10(1), 2589 (2019). doi:10.1038/s41467-019-10448-x, X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature., Published by Nature Publishing Group UK, [London]

43. Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements.

Author

Barty A, Caleman C, Aquila A, Timneanu N, Lomb L, White TA, Andreasson J, Arnlund D, Bajt S, Barends TR, Barthelmess M, Bogan MJ, Bostedt C, Bozek JD, Coffee R, Coppola N, Davidsson J, Deponte DP, Doak RB, Ekeberg T, Elser V, Epp SW, Erk B, Fleckenstein H, Foucar L, Fromme P, Graafsma H, Gumprecht L, Hajdu J, Hampton CY, Hartmann R, Hartmann A, Hauser G, Hirsemann H, Holl P, Hunter MS, Johansson L, Kassemeyer S, Kimmel N, Kirian RA, Liang M, Maia FR, Malmerberg E, Marchesini S, Martin AV, Nass K, Neutze R, Reich C, Rolles D, Rudek B, Rudenko A, Scott H, Schlichting I, Schulz J, Seibert MM, Shoeman RL, Sierra RG, Soltau H, Spence JC, Stellato F, Stern S, Strüder L, Ullrich J, Wang X, Weidenspointner G, Weierstall U, Wunderer CB, and Chapman HN

Abstract

X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis 1 . For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information 1-4 . Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology 5 should enable structural determination from submicrometre protein crystals with atomic resolution.

Published
2012
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