Lipidic cubic phase serial millisecond crystallography using synchrotron radiation
Artikel i vetenskaplig tidskrift, 2015

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.

protein crystallography

MACROMOLECULAR

Chemistry

CRYSTALLIZATION

Multidisciplinary

DAMAGE

lipidic cubic phases

FREE-ELECTRON

CRYSTALLOGRAPHY

XFEL

FEMTOSECOND CRYSTALLOGRAPHY

PROTEIN-STRUCTURE DETERMINATION

LASER

Materials Science

Multidisciplinary

Crystallography

MEMBRANE-PROTEINS

bacteriorhodopsin

RESOLUTION

X-RAY CRYSTALLOGRAPHY

SOFTWARE

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Publicerad i

IUCrJ

2052-2525 (eISSN)

Vol. 2 s. 168-176 Part: 2

Kategorisering

Ämneskategorier (SSIF 2011)

Kemi

Identifikatorer

DOI

10.1107/s2052252514026487

PubMed

25866654

Mer information

Skapat

2017-10-10