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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli.
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Using rational screening and electron microscopy to optimize the crystallization of succinate:ubiquinone oxidoreductase from Escherichia coli.

机译：使用rational筛查和电子显微镜优化的结晶琥珀酸:泛醌氧化还原酶大肠杆菌。

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摘要

The membrane-bound respiratory complex II, succinate:ubiquinone oxidoreductase (SQR) from Escherichia coli, has been anaerobically expressed, then purified and crystallized. The initial crystals obtained were small and diffracted poorly. In order to facilitate structure determination, rational screening and sample-quality analysis using electron microscopy was implemented. The crystals of SQR from E. coli belong to the trigonal space group R32, with unit-cell parameters a = b = 138.7, c = 521.9 A, and diffract to 2.6 A resolution. The optimization strategy used for obtaining well diffracting SQR crystals is applicable to a wide range of membrane proteins.
机译：膜结合呼吸复杂二世,琥珀酸:泛醌氧化还原酶(SQR)大肠杆菌、厌氧表达,纯化和结晶。最初的晶体是小而获得的衍射不佳。结构确定,理性的筛查和使用电子显微镜样品质量分析是实现的。属于三方晶系的空间群R32,晶胞参数a = b = 138.7, c = 521.9,2.6和衍射分辨率。优化策略用于获取晶体衍射SQR适用于宽膜蛋白。

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