Femtosecond X-ray protein nanocrystallography

被引:1641
|
作者
Chapman, Henry N. [1 ,2 ]
Fromme, Petra [3 ]
Barty, Anton [1 ]
White, Thomas A. [1 ]
Kirian, Richard A. [4 ]
Aquila, Andrew [1 ]
Hunter, Mark S. [3 ]
Schulz, Joachim [1 ]
DePonte, Daniel P. [1 ]
Weierstall, Uwe [4 ]
Doak, R. Bruce [4 ]
Maia, Filipe R. N. C. [5 ]
Martin, Andrew V. [1 ]
Schlichting, Ilme [6 ,7 ]
Lomb, Lukas [7 ]
Coppola, Nicola [1 ]
Shoeman, Robert L. [7 ]
Epp, Sascha W. [6 ,8 ]
Hartmann, Robert [9 ]
Rolles, Daniel [6 ,7 ]
Rudenko, Artem [6 ,8 ]
Foucar, Lutz [6 ,7 ]
Kimmel, Nils [10 ]
Weidenspointner, Georg [10 ,11 ]
Holl, Peter [9 ]
Liang, Mengning [1 ]
Barthelmess, Miriam
Caleman, Carl [1 ]
Boutet, Sebastien [12 ]
Bogan, Michael J. [13 ]
Krzywinski, Jacek [12 ]
Bostedt, Christoph [12 ]
Bajt, Sasa
Gumprecht, Lars [1 ]
Rudek, Benedikt [6 ,8 ]
Erk, Benjamin [6 ,8 ]
Schmidt, Carlo [6 ,8 ]
Hoemke, Andre [6 ,8 ]
Reich, Christian [9 ]
Pietschner, Daniel [10 ]
Strueder, Lothar [6 ,10 ]
Hauser, Guenter [10 ]
Gorke, Hubert [14 ]
Ullrich, Joachim [6 ,8 ]
Herrmann, Sven [10 ]
Schaller, Gerhard [10 ]
Schopper, Florian [10 ]
Soltau, Heike [9 ]
Kuehnel, Kai-Uwe [8 ]
Messerschmidt, Marc [12 ]
机构
[1] DESY, Ctr Free Electron Laser Sci, D-22607 Hamburg, Germany
[2] Univ Hamburg, D-22761 Hamburg, Germany
[3] Arizona State Univ, Dept Chem & Biochem, Tempe, AZ 85287 USA
[4] Arizona State Univ, Dept Phys, Tempe, AZ 85287 USA
[5] Uppsala Univ, Dept Cell & Mol Biol, Lab Mol Biophys, SE-75124 Uppsala, Sweden
[6] Max Planck Adv Study Grp, Ctr Free Electron Laser Sci, D-22607 Hamburg, Germany
[7] Max Planck Inst Med Res, D-69120 Heidelberg, Germany
[8] Max Planck Inst Kernphys, D-69117 Heidelberg, Germany
[9] PNSensor GmbH, D-81739 Munich, Germany
[10] Max Planck Inst Halbleiterlab, D-81739 Munich, Germany
[11] Max Planck Inst Extraterr Phys, D-85741 Garching, Germany
[12] SLAC Natl Accelerator Lab, LCLS, Menlo Pk, CA 94025 USA
[13] SLAC Natl Accelerator Lab, PULSE Inst, Menlo Pk, CA 94025 USA
[14] Forschungszentrum Julich, Inst ZEL, D-52425 Julich, Germany
[15] Lawrence Livermore Natl Lab, Livermore, CA 94551 USA
[16] Lawrence Berkeley Natl Lab, Adv Light Source, Berkeley, CA 94720 USA
[17] Univ Gothenburg, Dept Chem Biochem & Biophys, SE-40530 Gothenburg, Sweden
[18] Tech Univ Berlin, Inst Opt & Atomare Phys, D-10623 Berlin, Germany
[19] Swedish Univ Agr Sci, Uppsala Biomed Ctr, Dept Mol Biol, S-75124 Uppsala, Sweden
基金
瑞典研究理事会; 美国国家科学基金会; 美国国家卫生研究院;
关键词
REFINEMENT;
D O I
10.1038/nature09750
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 (similar to 200 nm to 2 mm 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.
引用
收藏
页码:73 / U81
页数:6
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