Journal Article PUBDB-2015-04290

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

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2015
AIP Publishing LLC Melville, NY

Structural dynamics 2(4), 041718 () [10.1063/1.4922774]
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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.

Classification:

Contributing Institute(s):
  1. CFEL-Coherent X-Ray Imaging (FS-CFEL-1)
Research Program(s):
  1. 6215 - Soft Matter, Health and Life Sciences (POF3-621) (POF3-621)
  2. NANOMEM - Membrane Protein Nanocrystallography (317079) (317079)
  3. X-probe - Advanced XFEL and Synchrotron based Probes of Protein Structure and Dynamics (637295) (637295)
  4. VH-GS-500 - PIER Helmholtz Graduate School (2015_IFV-VH-GS-500) (2015_IFV-VH-GS-500)
Experiment(s):
  1. Experiments at CFEL

Appears in the scientific report 2015
Database coverage:
Creative Commons Attribution CC BY 3.0 ; OpenAccess ; SCOPUS
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 Record created 2015-10-21, last modified 2025-07-30


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