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Time-resolved structural studies with serial crystallography: A new light on retinal proteins

Authors :
Valérie Panneels
Wenting Wu
Ching-Ju Tsai
Przemek Nogly
Jan Rheinberger
Kathrin Jaeger
Gregor Cicchetti
Cornelius Gati
Leonhard M. Kick
Leonardo Sala
Guido Capitani
Chris Milne
Celestino Padeste
Bill Pedrini
Xiao-Dan Li
Jörg Standfuss
Rafael Abela
Gebhard Schertler
Source :
Structural Dynamics, Vol 2, Iss 4, Pp 041718-041718-8 (2015)
Publication Year :
2015
Publisher :
AIP Publishing LLC and ACA, 2015.

Abstract

Structural information of the different conformational states of the two prototypical light-sensitive membrane proteins, bacteriorhodopsin and rhodopsin, has been obtained in the past by X-ray cryo-crystallography and cryo-electron microscopy. However, these methods do not allow for the structure determination of most intermediate conformations. Recently, the potential of X-Ray Free Electron Lasers (X-FELs) for tracking the dynamics of light-triggered processes by pump-probe serial femtosecond crystallography has been demonstrated using 3D-micron-sized crystals. In addition, X-FELs provide new opportunities for protein 2D-crystal diffraction, which would allow to observe the course of conformational changes of membrane proteins in a close-to-physiological lipid bilayer environment. Here, we describe the strategies towards structural dynamic studies of retinal proteins at room temperature, using injector or fixed-target based serial femtosecond crystallography at X-FELs. Thanks to recent progress especially in sample delivery methods, serial crystallography is now also feasible at synchrotron X-ray sources, thus expanding the possibilities for time-resolved structure determination.

Subjects

Subjects :
Crystallography
QD901-999

Details

Language :
English
ISSN :
23297778
Volume :
2
Issue :
4
Database :
Directory of Open Access Journals
Journal :
Structural Dynamics
Publication Type :
Academic Journal
Accession number :
edsdoj.bde68da3f8784c2bbd49084a306fd68f
Document Type :
article
Full Text :
https://doi.org/10.1063/1.4922774