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| Content Provider | PubMed Central |
|---|---|
| Author | Chapman, Henry N. Fromme, Petra Barty, Anton White, Thomas A. Kirian, Richard A. Aquila, Andrew Hunter, Mark S. Schulz, Joachim Deponte, Daniel P. Weierstall, Uwe Doak, R. Bruce Maia, Filipe R. N. C. Martin, Andrew V. Schlichting, Ilme Lomb, Lukas Coppola, Nicola Shoeman, Robert L. Epp, Sascha W. Hartmann, Robert Rolles, Daniel Rudenko, Artem Lutz, Foucar Kimmel, Nils Georg, Weidenspointner Holl, Peter Liang, Mengning Barthelmess, Miriam Carl, Caleman Boutet, Sébastien Bogan, Michael J. Jacek, Krzywinski Christoph, Bostedt Bajt, Saša Gumprecht, Lars Rudek, Benedikt Erk, Benjamin Schmidt, Carlo André, Hömke Reich, Christian Daniel, Pietschner Lothar, Strüder Hauser, Günter Gorke, Hubert Ullrich, Joachim Herrmann, Sven Schaller, Gerhard Schopper, Florian Soltau, Heike Kühnel, Kai-uwe Messerschmidt, Marc Bozek, John D. Hau-riege, Stefan P. Frank, Matthias Hampton, Christina Y. Sierra, Raymond G. Starodub, Dmitri Williams, Garth J. Hajdu, Janos Timneanu, Nicusor Seibert, M. Marvin Andreasson, Jakob Rocker, Andrea Jönsson, Olof Martin, Svenda Stern, Stephan Nass, Karol Robert, Andritschke Schröter, Claus-dieter Krasniqi, Faton Bott, Mario Schmidt, Kevin E. Wang, Xiaoyu Grotjohann, Ingo Holton, James M. Barends, Thomas R. M. Neutze, Richard Marchesini, Stefano Fromme, Raimund Sebastian, Schorb Rupp, Daniela Adolph, Marcus Tais, Gorkhover Andersson, Inger Hirsemann, Helmut Guillaume, Potdevin Heinz, Graafsma Nilsson, Björn Spence, John C. H. |
| Copyright Year | 2011 |
| Abstract | X-ray crystallography provides the vast majority of macromolecular structures, but the success of the method relies on growing crystals of sufficient size. In conventional measurements, the necessary increase in X-ray dose to record data from crystals that are too small leads to extensive damage before a diffraction signal can be recorded 1-3 . It is particularly challenging to obtain large, well-diffracting crystals of membrane proteins, for which fewer than 300 unique structures have been determined despite their importance in all living cells. Here we present a method for structure determination where single-crystal X-ray diffraction ‘snapshots’ are collected from a fully hydrated stream of nanocrystals using femtosecond pulses from a hard-X-ray free-electron laser, the Linac Coherent Light Source 4 . We prove this concept with nanocrystals of photosystem I, one of the largest membrane protein complexes 5 . More than 3,000,000 diffraction patterns were collected in this study, and a three-dimensional data set was assembled from individual photosystem I nanocrystals (~200 nm to 2 μm in size). We mitigate the problem of radiation damage in crystallography by using pulses briefer than the timescale of most damage processes 6 . This offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage. |
| Related Links | http://dx.doi.org/10.1038/nature09750 |
| Ending Page | 77 |
| Page Count | 5 |
| Starting Page | 73 |
| File Format | |
| ISSN | 00280836 |
| e-ISSN | 14764687 |
| Journal | Nature |
| Issue Number | 7332 |
| Volume Number | 470 |
| Language | English |
| Publisher Date | 2011-02-03 |
| Access Restriction | Open |
| Subject Keyword | General Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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