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000012877 084__ $$2WoS$$aBiochemical Research Methods
000012877 084__ $$2WoS$$aBiochemistry & Molecular Biology
000012877 084__ $$2WoS$$aBiophysics
000012877 084__ $$2WoS$$aCrystallography
000012877 1001_ $$0P:(DE-HGF)0$$aBorshchevskiy, V.$$b0
000012877 245__ $$aOvercoming merohedral twinning in crystals of bacteriorhodopsin grown in lipidic mesophase
000012877 260__ $$aCopenhagen$$bMunksgaard$$c2010
000012877 300__ $$a26 - 32
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000012877 440_0 $$056$$aActa Crystallographica D$$v66$$x0907-4449$$y1
000012877 500__ $$aThe work was supported by the program 'Chaires d'excellence' edition 2008 of ANR France, the CEA(IBS)-HGF(FZJ) STC 5.1 specific agreement and the MC grant for training and career development of researchers (Marie Curie, FP7-PEOPLE-2007-1-1-ITN, project SBMPs). This work was performed in the framework of Russian State Contracts Nos. 02.740.11.0299 (on the subject 'Cell biology and physical properties of membrane proteins' according to claim 'Scientific research by members of Research and Education Center in the field of physico-chemical molecular and cell biology', code 2009-1.1-142-064) and 02.740.11.5010 (on the subject 'Investigation of molecular mechanisms of the first step of energy transformation in the cell' according to claim 'Scientific research by groups under the guidance of invited scientists in the field of biology, agricultural science and living system technologies', code 2009-1.5-501-002) and a contract P974 on the subject of 'Ultrasensitive biosensors on the basis of nanomaterials' in the framework of activity 1.2.2 'Scientific research by scientific groups under the guidance of Candidates of Science' of the Federal Target Program 'Scientific and academic research cadres of innovative Russia' for 2009-2013. The authors would like to thank Christian Baeken, Maria Silacheva, Dmitry Bratanov, Yulia Borshchevskaya, Anton Abyzov, Alexandr Shava, Elizaveta Denisenko, Ivan Erofeev and Ivan Gushchin for their help with protein production and crystallization. Eva Pebay-Peyroula and Alexandr Popov are greatly acknowledged for their valuable comments on the manuscript.
000012877 520__ $$aTwinning is one of the most common crystal-growth defects in protein crystallography. There are neither efficient rational approaches for the growth of nontwinned protein crystals nor are there examples of systematic studies of the dependence of the twinning-ratio distribution on crystallization conditions. The description of the twinning phenomenon has been covered even less for membrane-protein crystals and is non-existent for crystals grown using lipidic phases (in meso). In the present work, possibilities for overcoming merohedral twinning are investigated for crystals of the membrane protein bacteriorhodopsin (bR) grown in meso. It is shown that traditional crystallization additives are not effective in the case of the in meso crystallization of bR. The twinning ratio was determined for 310 crystals grown under different crystallization conditions. A correlation of the twinning ratio with the growth rate of the crystals was observed. Slow growth indicated that crystals had a noticeable chance of avoiding twinning. Model calculations were performed in order to rationalize this observation. The calculations confirmed the experimental observation that most crystals consist of two twin domains and showed that under this condition small changes in the probability of twin-domain formation lead to dramatic changes in the number of nontwinned crystals, which explains why slow crystal growth results in a considerable number of nontwinned crystals.
000012877 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000012877 588__ $$aDataset connected to Web of Science, Pubmed
000012877 650_2 $$2MeSH$$aBacteriorhodopsins: chemistry
000012877 650_2 $$2MeSH$$aBacteriorhodopsins: isolation & purification
000012877 650_2 $$2MeSH$$aBacteriorhodopsins: metabolism
000012877 650_2 $$2MeSH$$aCrystallization
000012877 650_2 $$2MeSH$$aCrystallography, X-Ray
000012877 650_2 $$2MeSH$$aHalobacterium salinarum
000012877 650_2 $$2MeSH$$aLipids: chemistry
000012877 650_2 $$2MeSH$$aProtein Conformation
000012877 650_2 $$2MeSH$$aProtein Structure, Tertiary
000012877 650_2 $$2MeSH$$aPurple Membrane: metabolism
000012877 650_7 $$00$$2NLM Chemicals$$aLipids
000012877 650_7 $$053026-44-1$$2NLM Chemicals$$aBacteriorhodopsins
000012877 650_7 $$2WoSType$$aJ
000012877 7001_ $$0P:(DE-HGF)0$$aEfremov, R.$$b1
000012877 7001_ $$0P:(DE-HGF)0$$aMoiseeva, E.$$b2
000012877 7001_ $$0P:(DE-Juel1)131957$$aBüldt, G.$$b3$$uFZJ
000012877 7001_ $$0P:(DE-Juel1)VDB482$$aGordeliy, V. I.$$b4$$uFZJ
000012877 773__ $$0PERI:(DE-600)2020492-9$$a10.1107/S0907444909042838$$gVol. 66, p. 26 - 32$$p26 - 32$$q66<26 - 32$$tActa crystallographica / D$$v66$$x0907-4449$$y2010
000012877 8567_ $$uhttp://dx.doi.org/10.1107/S0907444909042838
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