Femtosecond X-ray diffraction from two-dimensional protein crystals
Category
Published on
Type
journal-article
Author
Matthias Frank and David B. Carlson and Mark S. Hunter and Garth J. Williams and Marc Messerschmidt and Nadia A. Zatsepin and Anton Barty and W. Henry Benner and Kaiqin Chu and Alexander T. Graf and Stefan P. Hau-Riege and Richard A. Kirian and Celestino Padeste and Tommaso Pardini and Bill Pedrini and Brent Segelke and M. Marvin Seibert and John C. H. Spence and Ching-Ju Tsai and Stephen M. Lane and Xiao-Dan Li and Gebhard Schertler and Sebastien Boutet and Matthew Coleman and James E. Evans
Citation
Frank, M. et al., 2014. Femtosecond X-ray diffraction from two-dimensional protein crystals. IUCrJ, 1(2), pp.95–100. Available at: http://dx.doi.org/10.1107/s2052252514001444.
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.
DOI
Funding
NSF-STC Biology with X-ray Lasers (NSF-1231306)