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

Författare

P. Nogly

D. James

D. J. Wang

T. A. White

N. Zatsepin

A. Shilova

G. Nelson

H. G. Liu

L. Johansson

M. Heymann

K. Jaeger

M. Metz

C. Wickstrand

W. T. Wu

P. Bath

Peter Berntsen

Göteborgs universitet

D. Oberthuer

V. Panneels

V. Cherezov

H. Chapman

G. Schertler

Richard Neutze

Göteborgs universitet

J. Spence

I. Moraes

M. Burghammer

J. Standfuss

U. Weierstall

IUCrJ

2052-2525 (eISSN)

Vol. 2 168-176 Part: 2

Ämneskategorier

Kemi

DOI

10.1107/s2052252514026487

PubMed

25866654