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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary X-ray analysis of the BRCT domains of human 53BP1 bound to the p53 tumour suppressor.
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Purification, crystallization and preliminary X-ray analysis of the BRCT domains of human 53BP1 bound to the p53 tumour suppressor.

机译:净化、结晶和初步的x射线分析BRCT人类53 bp1的域绑定到p53肿瘤抑制基因。

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摘要

A complex of the DNA-binding domain of the tumour suppressor p53 bound to the BRCT domains of the p53-binding protein (53BP1) has been prepared and purified. Single crystals have been obtained using the microbatch technique with polyethylene glycol 4 kDa and ammonium sulfate. Crystals diffract X-rays to beyond 2.3 A and belong to the space group P2(1)2(1)2(1). Several complete data sets have been collected from a number of crystals, each with different unit-cell parameters. Partial structures have been produced by successful placement of two copies of the p53 core region into the asymmetric unit. There is clear evidence for the binding protein and a complete structure determination is under way.
机译:一个复杂的dna结合域的肿瘤抑制基因p53绑定到BRCT域的p53-binding蛋白(53 bp1)已准备净化。使用与聚乙烯microbatch技术乙二醇4 kDa和硫酸铵。x射线衍射超出2.3,属于空间群P2(1) 2(1) 2(1)。集收集的水晶,每个都有不同的晶胞参数。p53的两个副本的成功的位置核心区域的不对称单元。结合蛋白和清晰的证据完整结构的决心。

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