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鸡胃G-肌动蛋白X脱氧核糖核酸酶I复合物在5埃分辨率下的晶体学研究。

Crystallographic studies of the chicken gizzard G-actin X DNase I complex at 5A resolution.

作者信息

Sakabe N, Sakabe K, Sasaki K, Kondo H, Ema T, Kamiya N, Matsushima M

出版信息

J Biochem. 1983 Jan;93(1):299-302. doi: 10.1093/oxfordjournals.jbchem.a134168.

Abstract

The structure of the chicken gizzard G-actin X DNase I complex has been determined at 5 A resolution by an X-ray diffraction method. Protein phases were computed by the multiple isomorphous replacement method using four heavy atom derivatives. The mean figure of merit was 0.65. Dimensions of the three molecular species, the complex, G-actin and DNase I, were determined based on the "cypress wood" models derived from the electron density map. The natures of the heavy atom binding sites are discussed in relation to the distinction between the two component molecules. The pattern of successive contacts between actin molecules observed in the present crystal seems unrelated to that found in F-actin.

摘要

鸡胗肌动蛋白X脱氧核糖核酸酶I复合物的结构已通过X射线衍射法在5埃分辨率下测定。使用四种重原子衍生物通过多同晶置换法计算蛋白质相位。平均品质因数为0.65。基于从电子密度图导出的“柏木”模型确定了三种分子种类(复合物、肌动蛋白和脱氧核糖核酸酶I)的尺寸。结合重原子位点的性质与两种组成分子之间的差异相关进行了讨论。在当前晶体中观察到的肌动蛋白分子之间连续接触的模式似乎与在F-肌动蛋白中发现的模式无关。

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