首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Purification crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii
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Purification crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii

机译:詹氏甲烷球菌CBS结构域蛋白MJ1004的纯化结晶和初步晶体学分析

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摘要

The purification and preliminary crystallographic analysis of the archaeal CBS-domain protein MJ1004 from Methanocaldococcus jannaschii are described. The native protein was overexpressed, purified and crystallized in the monoclinic space group P21, with unit-cell parameters a = 54.4, b = 53.8, c = 82.6 Å, β = 106.1°. The crystals diffracted X-rays to 2.7 Å resolution using synchrotron radiation. Matthews-volume calculations suggested the presence of two molecules in the asymmetric unit that are likely to correspond to a dimeric species, which is also observed in solution.
机译:描述了来自詹氏甲烷球菌的古细菌CBS结构域蛋白MJ1004的纯化和初步晶体学分析。天然蛋白质在单斜空间群P21中过表达,纯化和结晶,单位细胞参数a = 54.4,b = 53.8,c = 82.6Å,β= 106.1°。晶体使用同步加速器辐射将X射线衍射至2.7?Å分辨率。 Matthews-体积计算表明在不对称单元中存在两个分子,它们很可能对应于二聚体,这在溶液中也可以观察到。

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