Author:
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.
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.
Funder
National Institutes of Health
National Science Foundation
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,General Materials Science,Biochemistry,General Chemistry
Cited by
75 articles.
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