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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3.
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Purification, crystallization and preliminary crystallographic analysis of the glycine-cleavage system component T-protein from Pyrococcus horikoshii OT3.

机译:净化、结晶和初步的晶体glycine-cleavage的分析系统组件T-protein从海床

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摘要

The glycine-cleavage system component T-protein is a folate-dependent enzyme that catalyzes the formation of ammonia and 5,10-CH(2)-tetrahydrofolate from the aminomethyl intermediate bound to the lipoate cofactor of H-protein. T-protein from Pyrococcus horikoshii OT3 has been cloned, overexpressed in Escherichia coli, purified and crystallized by the microbatch method using PEG 4000 as a precipitant at 296 K. X-ray diffraction data have been collected to 1.50 A resolution at 100 K using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 78.980, b = 95.708, c = 118.331 A. Assuming one homodimer per asymmetric unit gives a V(M) value of 2.4 A(3) Da(-1) and a solvent content of 49.0%.
机译:组件T-protein glycine-cleavage系统folate-dependent酶催化的形成氨和5, 10-CH (2) -tetrahydrofolate氨甲基中间绑定到lipoate代数余子式的h型蛋白。OT3被克隆,过表达在大肠由microbatch杆菌、提纯和结晶方法使用4000作为沉淀剂在296 K挂钩。x射线衍射数据收集1.50使用同步加速器分辨率在100 K辐射。斜方晶系的空间群P2 (1) 2 (1) 2 (1)晶胞参数= 78.980,b = 95.708, c =118.331。单位给出了V (M)的价值(3)达2.4(1)和一个溶剂含量的49.0%。

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