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000005169 084__ $$2WoS$$aNanoscience & Nanotechnology
000005169 084__ $$2WoS$$aPhysics, Applied
000005169 084__ $$2WoS$$aPhysics, Condensed Matter
000005169 1001_ $$0P:(DE-HGF)0$$aMoiseeva, E.S.$$b0
000005169 245__ $$aComparative analysis of the quality of membrane protein bacteriorhodopsin crystals during crystallization in octylglucoside and octylthioglucoside
000005169 260__ $$aMoscow$$bMAIK Nauka/Interperiodics Publ.$$c2009
000005169 300__ $$a29 - 32
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000005169 440_0 $$019501$$aJournal of Surface Investigation : X-ray, Synchrotron and Neutron Techniques$$v3$$x1027-4510$$y1
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000005169 520__ $$aCrystallization of bacteriorhodopsin (bR) in the lipidic cubic phase using n-octyl-beta-D-glucoside (OG) and its more stable and inexpensive analogue n-octyl-beta-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 A...) than bR crystals in OTG (1.45 A...).
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000005169 7001_ $$0P:(DE-HGF)0$$aReshnetnyak, A.B.$$b1
000005169 7001_ $$0P:(DE-HGF)0$$aBorshchevskiy, V.I.$$b2
000005169 7001_ $$0P:(DE-Juel1)VDB59848$$aBaeken, C.$$b3$$uFZJ
000005169 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b4$$uFZJ
000005169 7001_ $$0P:(DE-Juel1)VDB482$$aGordeliy, V. I.$$b5$$uFZJ
000005169 773__ $$0PERI:(DE-600)2389417-9$$a10.1134/S1027451009010054$$gVol. 3, p. 29 - 32$$n1$$p29 - 32$$q3<29 - 32$$tJournal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques$$v3$$x1027-4510$$y2009
000005169 8567_ $$uhttp://dx.doi.org/10.1134/S1027451009010054
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