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000040230 0247_ $$2pmid$$apmid:15339801
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000040230 0247_ $$2DOI$$a10.1529/biophysj.104.046573
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000040230 084__ $$2WoS$$aBiophysics
000040230 1001_ $$0P:(DE-Juel1)VDB4616$$aEfremov, R.$$b0$$uFZJ
000040230 245__ $$aPhysical Detwinning of Hemihedrally Twinned Hexagonal Crystals of Bacteriorhdopsin
000040230 260__ $$aNew York, NY$$bRockefeller Univ. Press$$c2004
000040230 300__ $$a3608 - 3613
000040230 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000040230 440_0 $$0882$$aBiophysical Journal$$v87$$x0006-3495
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000040230 520__ $$aHexagonal crystals of the membrane protein bacteriorhodopsin of space group P6 3 grown in lipidic cubic phase are twinned hemihedrally. It was shown that slow changes of salt concentration in the mother liquor lead to a split of crystals so that the split parts preserved high diffraction quality. Analysis of diffraction data from split crystals by Yeates statistic and Britton plot showed that the split parts are free of twinning. It is concluded that crystals of bacteriorhodopsin are composed of several macroscopic twinning domains with sizes comparable to the original crystal. The appearance of twinning domains during crystal growth and the mechanism of splitting are discussed.
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000040230 650_2 $$2MeSH$$aBacteriorhodopsins: analysis
000040230 650_2 $$2MeSH$$aBacteriorhodopsins: chemistry
000040230 650_2 $$2MeSH$$aBacteriorhodopsins: ultrastructure
000040230 650_2 $$2MeSH$$aBinding Sites
000040230 650_2 $$2MeSH$$aComputer Simulation
000040230 650_2 $$2MeSH$$aCrystallization: methods
000040230 650_2 $$2MeSH$$aCrystallography: methods
000040230 650_2 $$2MeSH$$aModels, Chemical
000040230 650_2 $$2MeSH$$aModels, Molecular
000040230 650_2 $$2MeSH$$aMultiprotein Complexes: chemistry
000040230 650_2 $$2MeSH$$aMultiprotein Complexes: ultrastructure
000040230 650_2 $$2MeSH$$aProtein Binding
000040230 650_7 $$00$$2NLM Chemicals$$aMultiprotein Complexes
000040230 650_7 $$053026-44-1$$2NLM Chemicals$$aBacteriorhodopsins
000040230 650_7 $$2WoSType$$aJ
000040230 7001_ $$0P:(DE-Juel1)VDB8633$$aMoukhametzianov, R.$$b1$$uFZJ
000040230 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b2$$uFZJ
000040230 7001_ $$0P:(DE-Juel1)VDB482$$aGordeliy, V. I.$$b3$$uFZJ
000040230 773__ $$0PERI:(DE-600)1477214-0$$a10.1529/biophysj.104.046573$$gVol. 87, p. 3608 - 3613$$p3608 - 3613$$q87<3608 - 3613$$tBiophysical journal$$v87$$x0006-3495$$y2004
000040230 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1304826
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000040230 9141_ $$aNachtrag$$y2004
000040230 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000040230 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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