4X31 : Room temperature structure of bacteriorhodopsin from lipidic cubic phase obtained with serial millisecond crystallography using synchrotron radiation

  • Richard Neutze (Contributor)
  • Gebhard F X Schertler (Contributor)
  • Przemyslaw Nogly (Contributor)
  • Valerie Panneels (Contributor)
  • G. Nelson (Contributor)
  • Wenting Wu (Contributor)
  • Daniel James (Contributor)
  • Peter Berntsen (Contributor)
  • Henry N. Chapman (Contributor)
  • Thomas A. White (Contributor)
  • Uwe Weierstall (Contributor)
  • John Spence (Contributor)
  • Jörg Standfuss (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2015-02-18
Deposition Date:2014-11-27
Revision Date:2015-03-11#2015-04-22
Molecular Weight:28541.7
Macromolecule Type:Protein
Residue Count:229
Atom Site Count:1838

Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 Å. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway.
Date made available2015

Cite this