Back to Search
Start Over
Time-resolved structural studies with serial crystallography: A new light on retinal proteins
- Source :
- Structural Dynamics, Vol 2, Iss 4, Pp 041718-041718-8 (2015)
- Publication Year :
- 2015
- Publisher :
- AIP Publishing LLC and ACA, 2015.
-
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.
- Subjects :
- Crystallography
QD901-999
Subjects
Details
- Language :
- English
- ISSN :
- 23297778
- Volume :
- 2
- Issue :
- 4
- Database :
- Directory of Open Access Journals
- Journal :
- Structural Dynamics
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.bde68da3f8784c2bbd49084a306fd68f
- Document Type :
- article
- Full Text :
- https://doi.org/10.1063/1.4922774