Lipidic cubic phase serial millisecond crystallography using synchrotron radiation

• 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.

Ämnesord

NATURVETENSKAP  -- Kemi (hsv//swe)

NATURAL SCIENCES  -- Chemical Sciences (hsv//eng)

Nyckelord

lipidic cubic phases

protein crystallography

bacteriorhodopsin

XFEL

PROTEIN-STRUCTURE DETERMINATION

X-RAY CRYSTALLOGRAPHY

FREE-ELECTRON

LASER

FEMTOSECOND CRYSTALLOGRAPHY

MEMBRANE-PROTEINS

MACROMOLECULAR

CRYSTALLOGRAPHY

CRYSTALLIZATION

DAMAGE

RESOLUTION

SOFTWARE

Chemistry

Multidisciplinary

Crystallography

Materials Science

Multidisciplinary

protein crystallography

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