Journal
IUCRJ
Volume 2, Issue -, Pages 168-176Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2052252514026487
Keywords
lipidic cubic phases; protein crystallography; bacteriorhodopsin; XFEL
Funding
- Swedish Research Council
- Knut and Alice Wallenberg Foundation
- NIH grant [R01GM108635]
- Rontgen-Angstrom-Cluster project of the German Bundesministerium fur Bildung und Forschung (BMBF) [05K2012]
- NSF STC award [1231306]
- Wellcome Trust [WT089809]
- NIH award [025979]
- Swiss National Science Foundation grant [310030_153145, 31003A_141235]
- European Union under programme FP7-PEOPLE-ITN NanoMem
- Swiss National Science Foundation (SNF) [310030_153145, 31003A_141235] Funding Source: Swiss National Science Foundation (SNF)
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Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 angstrom. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway.
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