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Start Over Author "Malmerberg, Erik" Publisher uppsala universitet, fysikalisk kemi
12 results on '"Malmerberg, Erik"'

1. Ultrafast structural changes within a photosynthetic reaction centre

Author

Dods, Robert, Bath, Petra, Morozov, Dmitry, Gagner, Viktor Ahlberg, Arnlund, David, Luk, Hoi Ling, Kubel, Joachim, Maj, Michal, 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, Sebastien, Barty, Anton, Katona, Gergely, Groenhof, Gerrit, Branden, Gisela, Neutze, Richard, Dods, Robert, Bath, Petra, Morozov, Dmitry, Gagner, Viktor Ahlberg, Arnlund, David, Luk, Hoi Ling, Kubel, Joachim, Maj, Michal, 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, Sebastien, Barty, Anton, Katona, Gergely, Groenhof, Gerrit, Branden, Gisela, and Neutze, Richard

Abstract

Photosynthetic reaction centres harvest the energy content of sunlight by transporting electrons across an energy-transducing biological membrane. Here we use time-resolved serial femtosecond crystallography(1) using an X-ray free-electron laser(2) to observe light-induced structural changes in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds. Structural perturbations first occur at the special pair of chlorophyll molecules of the photosynthetic reaction centre that are photo-oxidized by light. Electron transfer to the menaquinone acceptor on the opposite side of the membrane induces a movement of this cofactor together with lower amplitude protein rearrangements. These observations reveal how proteins use conformational dynamics to stabilize the charge-separation steps of electron-transfer reactions. Time-resolved serial femtosecond crystallography is used to reveal the structural changes that stabilize the charge-separation steps of electron-transfer reactions in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds.

Published
2021
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2. 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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3. 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, Branden, Gisela, Neutze, Richard, 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, Branden, Gisela, and Neutze, Richard

Abstract

Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RCvir). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RCvir serial femtosecond crystallography (SFX) structure from 3.3-angstrom to 2.4-angstrom resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.

Published
2017
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4. 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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5. 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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6. 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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7. 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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8. 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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9. 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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10. 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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11. 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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12. 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 R. M., 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 R.N.C., 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, Soltau, Heike, Shoeman, Robert L., Sierra, Raymond, 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 C. H., Chapman, Henry N., Aquila, Andrew, Hunter, Mark S., Doak, R. Bruce, Kirian, Richard A., Fromme, Petra, White, Thomas A., Andreasson, Jakob, Arnlund, David, Bajt, Saša, Barends, Thomas R. M., 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 R.N.C., 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, Soltau, Heike, Shoeman, Robert L., Sierra, Raymond, 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 C. H., and Chapman, Henry N.

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
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