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Title: Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals

Journal Article · · IUCrJ

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 Å. 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.

Research Organization:
Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)
Sponsoring Organization:
USDOE National Nuclear Security Administration (NNSA)
Grant/Contract Number:
AC52-07NA27344
OSTI ID:
1437805
Alternate ID(s):
OSTI ID: 1557945
Report Number(s):
LLNL-JRNL-782409; IUCRAJ; PII: S2052252517017043
Journal Information:
IUCrJ, Journal Name: IUCrJ Vol. 5 Journal Issue: 1; ISSN 2052-2525
Publisher:
International Union of Crystallography (IUCr)Copyright Statement
Country of Publication:
United Kingdom
Language:
English
Citation Metrics:
Cited by: 9 works
Citation information provided by
Web of Science

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