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

Valérie Panneels | Zendy; Wenting Wu | Zendy; ChingJu Tsai | Zendy; Przemysław Nogły | Zendy; Jan Rheinberger | Zendy; K. Jaeger | Zendy; Gregor Cicchetti | Zendy; Cornelius Gati | Zendy; Leonhard M. Kick | Zendy; L. Sala | Zendy; Guido Capitani | Zendy; Christopher J. Milne | Zendy; Celestino Padeste | Zendy; Bill Pedrini | Zendy; Xiaodan Li | Zendy; Jörg Standfuss | Zendy; R. Abela | Zendy; Gebhard F. X. Schertler | Zendy

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

Author(s) -

Valérie Panneels,

Wenting Wu,

ChingJu Tsai,

Przemysław Nogły,

Jan Rheinberger,

K. Jaeger,

Gregor Cicchetti,

Cornelius Gati,

Leonhard M. Kick,

L. Sala,

Guido Capitani,

Christopher J. Milne,

Celestino Padeste,

Bill Pedrini,

Xiaodan Li,

Jörg Standfuss,

R. Abela,

Gebhard F. X. Schertler

Publication year - 2015

Publication title -

structural dynamics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.415

H-Index - 29

ISSN - 2329-7778

DOI - 10.1063/1.4922774

Subject(s) - bacteriorhodopsin , electron crystallography , femtosecond , crystallography , synchrotron , lipid bilayer , rhodopsin , x ray crystallography , chemistry , membrane protein , protein crystallization , diffraction , biophysics , laser , materials science , membrane , retinal , crystallization , electron diffraction , optics , physics , biology , biochemistry , organic chemistry

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

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