Purification, crystallization and initial X-ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella.

Chayen NE; Raftery J; Helliwell JRZagalsky PFBoggon TJ

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and initial X-ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella.

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Purification, crystallization and initial X-ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella.

机译：净化、结晶和最初的x射线虾青素的C1单元的分析的蛋白质、V600 chondrophore Velellavelella。

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The subunit C1 of the carotenoid-binding protein, V600, of the chondrophore Velella velella has been purified and crystallized. The crystals, which were grown by the vapour-diffusion method from ammonium sulfate as the major precipitant, diffract beyond 3 A and show little radiation damage over long periods (greater than 100 h) on a Cu Kalpha rotating-anode X-ray source. The space group of the crystals is P212121 with cell dimensions a = 42.0, b = 80.9, c = 110. 6 A.

机译：子单元的C1 carotenoid-binding蛋白质,的V600 chondrophore Velella Velella纯化和结晶。vapour-diffusion种植的方法从硫酸铵主要的沉淀剂,衍射超出3和没有辐射损害长期(大于100 h)一个铜Kalpha旋转阳极x射线源。晶体的空间群P212121细胞维a = 42.0, b = 80.9, c = 110。

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《Acta crystallographica.Section D. Biological crystallography》 |1999年第1期|266-268|共3页
作者
Chayen NE; Raftery J; Helliwell JRZagalsky PFBoggon TJ;
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Biophysics Section, The Blackett Laboratory, Imperial College of Science, Technology and Medicine, London SW7 2BZ, England.;

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正文语种英语
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Protein Conformation; ammonium sulfate; X-ray analysisCrystallographyAnimalscrystalscell dimensionsastaxanthineRadiation InjuriesX-raysCrystallization;

机译：蛋白质的构象,硫酸铵;x射线analysisCrystallographyAnimalscrystalscelldimensionsastaxanthineRadiationInjuriesX-raysCrystallization;

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Purification, crystallization and initial X-ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella.

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