Journal
IUCRJ
Volume 5, Issue -, Pages 103-117Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252517017043
Keywords
serial crystallography; free-electron lasers; membrane proteins; two-dimensional crystals
Funding
- US Department of Energy by Lawrence Livermore National Laboratory [DE-AC52-07NA27344]
- LLNL Laboratory-Directed Research and Development (LDRD) project [12-ERD-031]
- NIH grant [1R01GM117342-01]
- National Science Foundation [CBET-1264434, 1231306, 1565180]
- National Science Foundation (NSF-STC 'BioXFEL' award) [STC-1231306]
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- Direct For Biological Sciences
- Div Of Biological Infrastructure [1565180] Funding Source: National Science Foundation
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Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4 A. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.
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