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243 results on '"Neutze, R."'

4. Serial femtosecond crystallography structure of CO bound ba3- type cytochrome c oxidase at 2 milliseconds after irradiation by a 532 nm laser

Author

Safari, C., primary, Ghosh, S., additional, Andersson, R., additional, Johannesson, J., additional, Donoso, A.V., additional, Bath, P., additional, Bosman, R., additional, Dahl, P., additional, Nango, E., additional, Tanaka, R., additional, Zoric, D., additional, Svensson, E., additional, Nakane, T., additional, Iwata, S., additional, Neutze, R., additional, and Branden, G., additional

Published
2023
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20. New Science Opportunities Enabled by LCLS-II X-Ray Lasers

Author

Abbamonte, P., primary, Abild-Pedersen, Frank, additional, Adams, P., additional, Ahmed, M., additional, Albert, F., additional, Mori, R., additional, Anfinrud, P., additional, Aquila, A., additional, Armstrong, M., additional, Arthur, J., additional, Bargar, J., additional, Barty, A., additional, Bergmann, U., additional, Berrah, N., additional, Blaj, G., additional, Bluhm, H., additional, Bolme, C., additional, Bostedt, C., additional, Boutet, S., additional, Brown, G., additional, Bucksbaum, P., additional, Cargnello, M., additional, Carini, G., additional, Cavalleri, A., additional, Cherezov, V., additional, Chiu, W., additional, Chuang, Y., additional, Cocco, D., additional, Coffee, R., additional, Collins, G., additional, Cordones-Hahn, A., additional, Cryan, J., additional, Dakovski, G., additional, Dantus, M., additional, Demirci, H., additional, Denes, P., additional, Devereaux, T., additional, Ding, Y., additional, Doniach, S., additional, Dorner, R., additional, Dunne, M., additional, Durr, H., additional, Egami, T., additional, Eisenberg, D., additional, Emma, P., additional, Fadley, C., additional, Falcone, R., additional, Feng, Y., additional, Fischer, P., additional, Fiuza, F., additional, Fletcher, L., additional, Foucar, L., additional, Frank, M., additional, Fraser, J., additional, Frei, H., additional, Fritz, D., additional, Fromme, P., additional, Fry, A., additional, Fuchs, M., additional, Fuoss, P., additional, Gaffney, K., additional, Gamboa, E., additional, Gessner, O., additional, Ghimire, S., additional, Gleason, A., additional, Glenzer, S., additional, Gorkhover, T., additional, Gray, A., additional, Guehr, M., additional, Guo, J., additional, Hajdu, J., additional, Hansen, S., additional, Hart, P., additional, Hashimoto, M., additional, Hastings, J., additional, Haxton, D., additional, Heimann, P., additional, Heinz, T., additional, Hexemer, A., additional, Hill, J., additional, Himpsel, F., additional, Ho, P., additional, Hogue, B., additional, Huang, Z., additional, Hunter, M., additional, Hura, G., additional, Huse, N., additional, Hussain, Z., additional, Ilchen, M., additional, Jacobsen, C., additional, Kenney, C., additional, Kern, J., additional, Kevan, S., additional, Kim, J., additional, Kim, H., additional, Kirchmann, P., additional, Kirian, R., additional, Kivelson, S., additional, Kliewer, C., additional, Koralek, J., additional, Kovacsova, G., additional, Lanzara, A., additional, LaRue, J., additional, Lee, H., additional, Lee, J., additional, Lee, W., additional, Lee, Y., additional, Lindau, I., additional, Lindenberg, A., additional, Liu, Z., additional, Lu, D., additional, Lundstrom, U., additional, MacDowell, A., additional, Mao, W., additional, Marangos, J., additional, Marcus, G., additional, Martinez, T., additional, McCurdy, W., additional, McDermott, G., additional, McGuffey, C., additional, Minitti, M., additional, Miyabe, S., additional, Moeller, S., additional, Moore, R., additional, Mukamel, S., additional, Nass, K., additional, Natan, A., additional, Nelson, K., additional, Nemsak, S., additional, Neumark, D., additional, Neutze, R., additional, Nilsson, A., additional, Nordlund, D., additional, Norskov, J., additional, Nozawa, S., additional, Ogasawara, H., additional, Ohldag, H., additional, Orville, A., additional, Osborn, D., additional, Osipov, T., additional, Ourmazd, A., additional, Parkinson, D., additional, Pellegrini, C., additional, Phillips, G., additional, Rasing, T., additional, Raubenheimer, T., additional, Recigno, T., additional, Reid, A., additional, Reis, D., additional, Robert, A., additional, Robinson, J., additional, Rolles, D., additional, Rost, J., additional, Roy, S., additional, Rudenko, A., additional, Russell, T., additional, Sandberg, R., additional, Sandhu, A., additional, Sauter, N., additional, Schlichting, I., additional, Schlogl, R., additional, Schlotter, W., additional, Schmidt, M., additional, Schneider, J., additional, Schoenlein, R., additional, Schoeffler, M., additional, Scholl, A., additional, Shen, Z., additional, Shpyrko, O., additional, Silva, T., additional, Sinha, S., additional, Slaughter, D., additional, Sobota, J., additional, Sokaras, D., additional, Sokolowski-Tinten, K., additional, Southworth, S., additional, Spence, J., additional, Stan, C., additional, Stohr, J., additional, Stroud, R., additional, Sundstrom, V., additional, Taatjes, C., additional, Thomas, A., additional, Trigo, M., additional, Tsui, Y., additional, Turner, J., additional, van Buuren, A., additional, Vinko, S., additional, Wakatsuki, S., additional, Wark, J., additional, Weber, P., additional, Weber, T., additional, Wei, M., additional, Weiss, T., additional, Wernet, P., additional, White, W., additional, Willmott, P., additional, Wilson, K., additional, Wurth, W., additional, Yachandra, V., additional, Yano, J., additional, Yarotski, D., additional, Young, L., additional, Zhu, Y., additional, Zhu, D., additional, and Zwart, P., additional

Published
2015
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21. Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: resting state structure

Author

Nogly, P., primary, Weinert, T., additional, James, D., additional, Cabajo, S., additional, Ozerov, D., additional, Furrer, A., additional, Gashi, D., additional, Borin, V., additional, Skopintsev, P., additional, Jaeger, K., additional, Nass, K., additional, Bath, P., additional, Bosman, R., additional, Koglin, J., additional, Seaberg, M., additional, Lane, T., additional, Kekilli, D., additional, Bruenle, S., additional, Tanaka, T., additional, Wu, W., additional, Milne, C., additional, White, T., additional, Barty, A., additional, Weierstall, U., additional, Panneels, V., additional, Nango, E., additional, Iwata, S., additional, Hunter, M., additional, Schapiro, I., additional, Schertler, G., additional, Neutze, R., additional, and Standfuss, J., additional

Published
2018
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22. Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 49-406 fs state structure

Author

Nogly, P., primary, Weinert, T., additional, James, D., additional, Cabajo, S., additional, Ozerov, D., additional, Furrer, A., additional, Gashi, D., additional, Borin, V., additional, Skopintsev, P., additional, Jaeger, K., additional, Nass, K., additional, Bath, P., additional, Bosman, R., additional, Koglin, J., additional, Seaberg, M., additional, Lane, T., additional, Kekilli, D., additional, Bruenle, S., additional, Tanaka, T., additional, Wu, W., additional, Milne, C., additional, White, T., additional, Barty, A., additional, Weierstall, U., additional, Panneels, V., additional, Nango, E., additional, Iwata, S., additional, Hunter, M., additional, Schapiro, I., additional, Schertler, G., additional, Neutze, R., additional, and Standfuss, J., additional

Published
2018
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23. Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 457-646 fs state structure

Author

Nogly, P., primary, Weinert, T., additional, James, D., additional, Cabajo, S., additional, Ozerov, D., additional, Furrer, A., additional, Gashi, D., additional, Borin, V., additional, Skopintsev, P., additional, Jaeger, K., additional, Nass, K., additional, Bath, P., additional, Bosman, R., additional, Koglin, J., additional, Seaberg, M., additional, Lane, T., additional, Kekilli, D., additional, Bruenle, S., additional, Tanaka, T., additional, Wu, W., additional, Milne, C., additional, White, T., additional, Barty, A., additional, Weierstall, U., additional, Panneels, V., additional, Nango, E., additional, Iwata, S., additional, Hunter, M., additional, Schapiro, I., additional, Schertler, G., additional, Neutze, R., additional, and Standfuss, J., additional

Published
2018
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24. Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 8.3 ms state structure

Author

Nogly, P., primary, Weinert, T., additional, James, D., additional, Cabajo, S., additional, Ozerov, D., additional, Furrer, A., additional, Gashi, D., additional, Borin, V., additional, Skopintsev, P., additional, Jaeger, K., additional, Nass, K., additional, Bath, P., additional, Bosman, R., additional, Koglin, J., additional, Seaberg, M., additional, Lane, T., additional, Kekilli, D., additional, Bruenle, S., additional, Tanaka, T., additional, Wu, W., additional, Milne, C., additional, White, T., additional, Barty, A., additional, Weierstall, U., additional, Panneels, V., additional, Nango, E., additional, Iwata, S., additional, Hunter, M., additional, Schapiro, I., additional, Schertler, G., additional, Neutze, R., additional, and Standfuss, J., additional

Published
2018
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25. Retinal isomerization in bacteriorhodopsin revealed by a femtosecond X-ray laser: 10 ps state structure

Author

Nogly, P., primary, Weinert, T., additional, James, D., additional, Cabajo, S., additional, Ozerov, D., additional, Furrer, A., additional, Gashi, D., additional, Borin, V., additional, Skopintsev, P., additional, Jaeger, K., additional, Nass, K., additional, Bath, P., additional, Bosman, R., additional, Koglin, J., additional, Seaberg, M., additional, Lane, T., additional, Kekilli, D., additional, Bruenle, S., additional, Tanaka, T., additional, Wu, W., additional, Milne, C., additional, White, T., additional, Barty, A., additional, Weierstall, U., additional, Panneels, V., additional, Nango, E., additional, Iwata, S., additional, Hunter, M., additional, Schapiro, I., additional, Schertler, G., additional, Neutze, R., additional, and Standfuss, J., additional

Published
2018
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26. X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate

Author

Wilmouth, RC, Edman, K, Neutze, R, Wright, PA, Clifton, IJ, Schneider, TR, Schofield, CJ, and Hajdu, J

Abstract

Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues. An oxyanion hole, consisting of the peptide amide of the active site serine and a neighbouring glycine, was identified, and hydrogen bonding in the oxyanion hole was suggested to stabilize the two proposed tetrahedral intermediates on the catalytic pathway. Here we show electron density changes consistent with the formation of a tetrahedral intermediate during the hydrolysis of an acyl-enzyme complex formed between a natural heptapeptide and elastase. No electron density for an enzyme-product complex was observed. The structures also suggest a mechanism for the synchronization of hydrolysis and peptide release triggered by the conversion of the sp2 hybridized carbonyl carbon to an sp3 carbon in the tetrahedral intermediate. This affects the location of the peptide in the active site cleft, triggering the collapse of a hydrogen bonding network between the peptide and the beta-sheet of the active site.

Published
2016

27. Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography

Author

Andersson, R., primary, Safari, C., additional, Dods, R., additional, Nango, E., additional, Tanaka, R., additional, Nakane, T., additional, Tono, K., additional, Joti, Y., additional, Bath, P., additional, Dunevall, E., additional, Bosman, E., additional, Nureki, O., additional, Iwata, S., additional, Neutze, R., additional, and Branden, G., additional

Published
2017
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44. Bacteriorhodopsin ground state structure obtained with Serial Femtosecond Crystallography

Author

Nogly, P., primary, Panneels, V., additional, Nelson, G., additional, Gati, C., additional, Kimura, T., additional, Milne, C., additional, Milathianaki, D., additional, Kubo, M., additional, Wu, W., additional, Conrad, C., additional, Coe, J., additional, Bean, R., additional, Zhao, Y., additional, Bath, P., additional, Dods, R., additional, Harimoorthy, R., additional, Beyerlein, K.R., additional, Rheinberger, J., additional, James, D., additional, DePonte, D., additional, Li, C., additional, Sala, L., additional, Williams, G., additional, Hunter, M., additional, Koglin, J.E., additional, Berntsen, P., additional, Nango, E., additional, Iwata, S., additional, Chapman, H.N., additional, Fromme, P., additional, Frank, M., additional, Abela, R., additional, Boutet, S., additional, Barty, A., additional, White, T.A., additional, Weierstall, U., additional, Spence, J., additional, Neutze, R., additional, Schertler, G., additional, and Standfuss, J., additional

Published
2016
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46. Conformational activation of visual rhodopsin in native disc membranes

Author

Malmerberg, E., Bovee-Geurts, P.H.M., Katona, G., Deupi, X., Arnlund, D., Wickstrand, C., Johansson, L.C., Westenhoff, S., Nazarenko, E., GF, X.S., Menzel, A., Grip, W.J. de, Neutze, R., Malmerberg, E., Bovee-Geurts, P.H.M., Katona, G., Deupi, X., Arnlund, D., Wickstrand, C., Johansson, L.C., Westenhoff, S., Nazarenko, E., GF, X.S., Menzel, A., Grip, W.J. de, and Neutze, R.

Abstract

Contains fulltext : 154870.pdf (publisher's version ) (Closed access), Rhodopsin is the G protein-coupled receptor (GPCR) that serves as a dim-light receptor for vision in vertebrates. We probed light-induced conformational changes in rhodopsin in its native membrane environment at room temperature using time-resolved wide-angle x-ray scattering. We observed a rapid conformational transition that is consistent with an outward tilt of the cytoplasmic portion of transmembrane helix 6 concomitant with an inward movement of the cytoplasmic portion of transmembrane helix 5. These movements were considerably larger than those reported from the basis of crystal structures of activated rhodopsin, implying that light activation of rhodopsin involves a more extended conformational change than was previously suggested.

Published
2015

47. Native inhibition of Trypanosoma brucei cathepsin B revealed by an X-ray laser at 2.1 \u01fa resolution

Author

Redecke L, Nass K, DePonte DP, White TA, Rehders D, Barty A, Stellato F, Liang M, Barends TRM, Boutet S, Williams GJ, Messerschmidt M, Seibert MM, Aquila A, Arnlund D, Bajt S, Barth T, Bogan MJ, Caleman C, Chao T, Doak RB, Fleckenstein H, Frank M, Fromme R, Galli L, Grotjohann I, Hunter MS, Johansson LC, Kassemeyer S, Katona G, Kirian R, Koopmann R, Kupitz C, Lomb L, Martin AV, Mogk S, Neutze R, Shoeman RL, Steinbrener J, Timneanu N, Wang D, Weierstall U, Zatsepin NA, Spence JCH, Fromme P, and Schlichting I

Published
2013

49. Room temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation

Author

Nogly, P., primary, James, D., additional, Wang, D., additional, White, T., additional, Zatsepin, N., additional, Shilova, A., additional, Nelson, G., additional, Liu, H., additional, Johansson, L., additional, Heymann, M., additional, Jaeger, K., additional, Metz, M., additional, Wickstrand, C., additional, Wu, W., additional, Baath, P., additional, Berntsen, P., additional, Oberthuer, D., additional, Panneels, V., additional, Cherezov, V., additional, Chapman, H., additional, Spence, J., additional, Schertler, G., additional, Neutze, R., additional, Moraes, I., additional, Burghammer, M., additional, Standfuss, J., additional, and Weierstall, U., additional

Published
2015
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50. X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking

Author

Frick, A., Eriksson, U.K., Mattia, F.P. de, Oberg, F., Hedfalk, K., Neutze, R., Grip, W.J. de, Deen, P.M.T., Tornroth-Horsefield, S., Frick, A., Eriksson, U.K., Mattia, F.P. de, Oberg, F., Hedfalk, K., Neutze, R., Grip, W.J. de, Deen, P.M.T., and Tornroth-Horsefield, S.

Abstract

Contains fulltext : 133922.pdf (publisher's version ) (Open Access), Human aquaporin 2 (AQP2) is a water channel found in the kidney collecting duct, where it plays a key role in concentrating urine. Water reabsorption is regulated by AQP2 trafficking between intracellular storage vesicles and the apical membrane. This process is tightly controlled by the pituitary hormone arginine vasopressin and defective trafficking results in nephrogenic diabetes insipidus (NDI). Here we present the X-ray structure of human AQP2 at 2.75 A resolution. The C terminus of AQP2 displays multiple conformations with the C-terminal alpha-helix of one protomer interacting with the cytoplasmic surface of a symmetry-related AQP2 molecule, suggesting potential protein-protein interactions involved in cellular sorting of AQP2. Two Cd(2+)-ion binding sites are observed within the AQP2 tetramer, inducing a rearrangement of loop D, which facilitates this interaction. The locations of several NDI-causing mutations can be observed in the AQP2 structure, primarily situated within transmembrane domains and the majority of which cause misfolding and ER retention. These observations provide a framework for understanding why mutations in AQP2 cause NDI as well as structural insights into AQP2 interactions that may govern its trafficking.

Published
2014

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