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

نویسندگان

  • 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
چکیده

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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عنوان ژورنال:

دوره 2  شماره 

صفحات  -

تاریخ انتشار 2015