1. Femtosecond X-ray diffraction from two-dimensional protein crystals
- Author
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Frank, Matthias, Carlson, David B, Hunter, Mark S, Williams, Garth J, Messerschmidt, Marc, Zatsepin, Nadia A, Barty, Anton, Benner, W Henry, Chu, Kaiqin, Graf, Alexander T, Hau-Riege, Stefan P, Kirian, Richard A, Padeste, Celestino, Pardini, Tommaso, Pedrini, Bill, Segelke, Brent, Seibert, M Marvin, Spence, John C H, Tsai, Ching-Ju, Lane, Stephen M, Li, Xiao-Dan, Schertler, Gebhard, Boutet, Sebastien, Coleman, Matthew, Evans, James E, Frank, Matthias, Carlson, David B, Hunter, Mark S, Williams, Garth J, Messerschmidt, Marc, Zatsepin, Nadia A, Barty, Anton, Benner, W Henry, Chu, Kaiqin, Graf, Alexander T, Hau-Riege, Stefan P, Kirian, Richard A, Padeste, Celestino, Pardini, Tommaso, Pedrini, Bill, Segelke, Brent, Seibert, M Marvin, Spence, John C H, Tsai, Ching-Ju, Lane, Stephen M, Li, Xiao-Dan, Schertler, Gebhard, Boutet, Sebastien, Coleman, Matthew, and Evans, James E
- Abstract
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 Å 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.
- Published
- 2014
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