Femtosecond X-ray diffraction from two-dimensional protein crystals

被引：64

作者：

Frank, Matthias ^{[1
]}

Carlson, David B. ^{[2
]}

Hunter, Mark S. ^{[1
]}

Williams, Garth J. ^{[3
]}

Messerschmidt, Marc ^{[3
]}

Zatsepin, Nadia A. ^{[4
]}

Barty, Anton ^{[5
]}

Benner, W. Henry ^{[1
]}

Chu, Kaiqin ^{[6
]}

Graf, Alexander T. ^{[1
]}

Hau-Riege, Stefan P. ^{[1
]}

Kirian, Richard A. ^{[5
]}

Padeste, Celestino ^{[7
]}

Pardini, Tommaso ^{[1
]}

Pedrini, Bill ^{[7
]}

Segelke, Brent ^{[1
]}

Seibert, M. Marvin ^{[3
]}

Spence, John C. H. ^{[4
]}

Tsai, Ching-Ju ^{[7
]}

Lane, Stephen M. ^{[6
]}

Li, Xiao-Dan ^{[7
]}

Schertler, Gebhard ^{[7
]}

Boutet, Sebastien ^{[3
]}

Coleman, Matthew ^{[1
]}

Evans, James E. ^{[2
,8
]}

机构：

[1] Lawrence Livermore Natl Lab, Livermore, CA 94550 USA

[2] Univ Calif Davis, Dept Mol & Cellular Biol, Davis, CA 95616 USA

[3] Linac Coherent Light Source, Menlo Pk, CA 94025 USA

[4] Arizona State Univ, Tempe, AZ 85287 USA

[5] Univ Hamburg, Ctr Free Electron Laser Sci, D-22761 Hamburg, Germany

[6] Ctr Biophoton, Sacramento, CA 95817 USA

[7] Paul Scherrer Inst, CH-5232 Villigen, Switzerland

[8] Pacific NW Natl Lab, Environm Mol Sci Lab, Richland, WA 99354 USA

来源：

IUCRJ | 2014年 / 1卷

基金：

美国国家科学基金会;

关键词：

two-dimensional protein crystal; femtosecond crystallography; single layer X-ray diffraction; membrane protein; BACTERIORHODOPSIN; CRYSTALLIZATION; MONOLAYERS; MODEL;

D O I：

10.1107/S2052252514001444

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 angstrom resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.

引用

页码：95 / 100

页数：6

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