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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba(3) oxidase from Thermus thermophilus
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A novel cryoprotection scheme for enhancing the diffraction of crystals of recombinant cytochrome ba(3) oxidase from Thermus thermophilus

机译：为提高小说cryoprotection模式晶体的衍射重组细胞色素ba(3)氧化酶从栖热菌属酸奶

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摘要

Cytochrome ba(3) oxidase is an integral membrane protein identified in the thermophilic bacterium Thermus thermophilus. The enzyme has now been expressed recombinantly and purified with a histidine tag. As such, it crystallizes under similar conditions and in the same space group (P4(3)2(1)2) as the native protein. A novel cryoprotection scheme is described here to obtain high-resolution diffraction from these crystals, which involves soaking in a mixture of glycerol and ethylene glycol under a layer of oil. The unit-cell parameters for these crystals are larger than the native protein, apparently deriving from increased ordering of the N-terminus and an internal loop (residues 495500) in subunit I. Hence, compared with native cytochrome ba3 oxidase, the recombinant His-tagged protein is accommodated in an expanded but equally well ordered lattice via an alternate set of specific intermolecular contacts. The structure was refined against data to 2.3 Angstrom resolution to an R factor of 21.7% and an R-free of 23.7%.
机译：英航(3)细胞色素氧化酶膜是一个积分嗜热细菌蛋白质鉴定栖热菌属酸奶。重组表达和纯化组氨酸标签。类似的条件和在同一空间群(P4(3) 2(1) 2)作为本机的蛋白质。这里描述cryoprotection方案获得高分辨率从这些晶体衍射,其中包括浸泡在甘油的混合物和乙二醇在一层油。这些晶体的晶胞参数明显大于原生蛋白质,从增加订购的n端和一个内部循环(495500年残留)在亚基。因此,相比之下,原住民细胞色素ba3氧化酶,重组His-tagged蛋白质是容纳在一个扩展但同样通过另一种有序的晶格组特定的分子间的联系人。2.3结构完善与数据21.7%的R因子和埃分辨率有空了23.7%。

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