Comparative analysis of the quality of membrane protein bacteriorhodopsin crystals during crystallization in octylglucoside and octylthioglucoside

  • E. S. Moiseeva
  • A. B. Reshetnyak
  • V. I. Borshchevskiy
  • C. Baeken
  • G. Buldt
  • V. I. Gordeliy
Article

DOI: 10.1134/S1027451009010054

Cite this article as:
Moiseeva, E.S., Reshetnyak, A.B., Borshchevskiy, V.I. et al. J. Synch. Investig. (2009) 3: 29. doi:10.1134/S1027451009010054

Abstract

Crystallization of bacteriorhodopsin (bR) in the lipidic cubic phase using n-octyl-β-D-glucoside (OG) and its more stable and inexpensive analogue n-octyl-β-D-thioglucoside (OTG) was comparatively analyzed [1]. It was shown that bacteriorhodopsin is efficiently crystallized in OTG in the same detergent concentration range as in OG. However, x-ray diffraction analysis shows that bR crystals in OG are characterized by a better resolution (1.35 Å) than bR crystals in OTG (1.45 Å).

Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • E. S. Moiseeva
    • 1
    • 2
  • A. B. Reshetnyak
    • 1
    • 2
  • V. I. Borshchevskiy
    • 1
    • 2
  • C. Baeken
    • 4
  • G. Buldt
    • 4
  • V. I. Gordeliy
    • 1
    • 2
    • 3
    • 4
  1. 1.Institut de Biologie Structurale J.P. EbelGrenoble Cedex 1France
  2. 2.Moscow Institute for Physics and TechnologyCentre of Biophysics and Physical Chemistry of Supramolecular StructuresDolgoprudnyi, Moscow oblastRussia
  3. 3.Frank Laboratory of Neutron PhysicsJoint Institute for Nuclear ResearchDubna, Moscow oblastRussia
  4. 4.Institute for Neurobiology and Biophysics 2Forschungszentrum JülichJülichGermany