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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization of Escherichia coli RuvA complexed with a synthetic Holliday junction.
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Crystallization of Escherichia coli RuvA complexed with a synthetic Holliday junction.

机译:结晶的大肠杆菌RuvA复杂化合成霍利迪结。

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During homologous recombination in Escherichia coli the RuvA, B and C proteins interact specifically with the Holliday junction formed by the action of RecA to promote the strand-exchange reaction. RuvA, a homotetrameric protein of molecular weight 88 kDa, has been overexpressed in E. coli, purified and co-crystallized with a synthetic Holliday junction substrate made from four 18-base deoxyoligonucleotides. Crystals were grown using the hanging-drop vapour-diffusion method with sodium acetate as the precipitant. The crystals diffract to a resolution of 6 A and belong to the monoclinic system, space group C2, with cell parameters a = 148, b = 148, c = 106 A and beta = 123 degrees. The X-ray analysis of these crystals should reveal the structure of the Holliday junction and its mode of binding to RuvA, providing new insights into the molecular mechanism of genetic recombination.
机译:在同源重组大肠杆菌RuvA, B和C蛋白相互作用特别是霍利迪结而形成的RecA促进strand-exchange的作用的反应。分子量88 kDa,过表达在大肠杆菌中,纯化和co-crystallized合成霍利迪结底物制成四个18-base deoxyoligonucleotides。增加使用悬滴vapour-diffusion方法以乙酸钠为沉淀剂。晶体衍射分辨率为6,属于单斜晶系,空间群C2,与细胞参数= 148,b = 148, c = 106和β= 123度。这些晶体应该揭示的结构霍利迪结及其模式绑定RuvA,提供分子的新见解基因重组机制。

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