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024 7 _ |2 DOI
|a 10.1134/S1027451009010054
024 7 _ |2 WOS
|a WOS:000263782100005
024 7 _ |2 ISSN
|a 1027-4510
037 _ _ |a PreJuSER-5169
041 _ _ |a eng
082 _ _ |a 530
084 _ _ |2 WoS
|a Nanoscience & Nanotechnology
084 _ _ |2 WoS
|a Physics, Applied
084 _ _ |2 WoS
|a Physics, Condensed Matter
100 1 _ |a Moiseeva, E.S.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Comparative analysis of the quality of membrane protein bacteriorhodopsin crystals during crystallization in octylglucoside and octylthioglucoside
260 _ _ |c 2009
|a Moscow
|b MAIK Nauka/Interperiodics Publ.
300 _ _ |a 29 - 32
336 7 _ |a Journal Article
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336 7 _ |a article
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440 _ 0 |a Journal of Surface Investigation : X-ray, Synchrotron and Neutron Techniques
|x 1027-4510
|0 19501
|y 1
|v 3
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Crystallization 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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650 _ 7 |a J
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700 1 _ |a Reshnetnyak, A.B.
|b 1
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700 1 _ |a Borshchevskiy, V.I.
|b 2
|0 P:(DE-HGF)0
700 1 _ |a Baeken, C.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB59848
700 1 _ |a Büldt, G.
|b 4
|u FZJ
|0 P:(DE-Juel1)131957
700 1 _ |a Gordeliy, V. I.
|b 5
|u FZJ
|0 P:(DE-Juel1)VDB482
773 _ _ |0 PERI:(DE-600)2389417-9
|a 10.1134/S1027451009010054
|g Vol. 3, p. 29 - 32
|p 29 - 32
|q 3<29 - 32
|t Journal of Surface Investigation. X-ray, Synchrotron and Neutron Techniques
|v 3
|x 1027-4510
|y 2009
|n 1
856 7 _ |u http://dx.doi.org/10.1134/S1027451009010054
909 C O |o oai:juser.fz-juelich.de:5169
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|d 31.12.2010
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