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

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 de...

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Veröffentlicht in:Structural dynamics (Melville, N.Y.) N.Y.), 2015-07, Vol.2 (4), p.041718-041718
Hauptverfasser: Panneels, Valérie, Wu, Wenting, Tsai, Ching-Ju, Nogly, Przemek, Rheinberger, Jan, Jaeger, Kathrin, Cicchetti, Gregor, Gati, Cornelius, Kick, Leonhard M, Sala, Leonardo, Capitani, Guido, Milne, Chris, Padeste, Celestino, Pedrini, Bill, Li, Xiao-Dan, Standfuss, Jörg, Abela, Rafael, Schertler, Gebhard
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Sprache:eng
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Zusammenfassung: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.
ISSN:2329-7778
2329-7778
DOI:10.1063/1.4922774