TY  - JOUR
AU  - Panneels, Valérie
AU  - Wu, Wenting
AU  - Tsai, Ching-Ju
AU  - Nogly, Przemek
AU  - Rheinberger, Jan
AU  - Jaeger, Kathrin
AU  - Cicchetti, Gregor
AU  - Gati, Cornelius
AU  - Kick, Leonhard M.
AU  - Sala, Leonardo
AU  - Capitani, Guido
AU  - Milne, Chris
AU  - Padeste, Celestino
AU  - Pedrini, Bill
AU  - Li, Xiao-Dan
AU  - Standfuss, Jörg
AU  - Abela, Rafael
AU  - Schertler, Gebhard
TI  - Time-resolved structural studies with serial crystallography: A new light on retinal proteins
JO  - Structural dynamics
VL  - 2
IS  - 4
SN  - 2329-7778
CY  - Melville, NY
PB  - AIP Publishing LLC
M1  - PUBDB-2015-04290
SP  - 041718
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000360649200020
C6  - pmid:26798817
DO  - DOI:10.1063/1.4922774
UR  - https://bib-pubdb1.desy.de/record/275873
ER  -