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Comparative analysis of the quality of membrane protein bacteriorhodopsin crystals during crystallization in octylglucoside and octylthioglucoside |
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| Authors: | E S Moiseeva A B Reshetnyak V I Borshchevskiy C Baeken G Buldt V I Gordeliy |
| Institution: | 1. Institut de Biologie Structurale J.P. Ebel, 41, rue Jules Horowitz, F-38027, Grenoble Cedex 1, France 2. Moscow Institute for Physics and Technology, Centre of Biophysics and Physical Chemistry of Supramolecular Structures, Institutskii per. 9, Dolgoprudnyi, Moscow oblast, 141700, Russia 4. Institute for Neurobiology and Biophysics 2, Forschungszentrum Jülich, 52425, Jülich, Germany 3. Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, ul. Zholio Kyuri 6, Dubna, Moscow oblast, 141980, Russia |
| 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). |
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