詹氏甲烷球菌CBS结构域蛋白MJ1004的纯化、结晶及初步晶体学分析
Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii.
作者信息
Oyenarte Iker, Lucas María, Gómez García Inmaculada, Martínez-Cruz Luis Alfonso
机构信息
Structural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia, Edificio 800, 48160 Derio, Bizkaia, Spain.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt 3):318-24. doi: 10.1107/S1744309110053479. Epub 2011 Feb 23.
Abstract
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 P2(1), 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.
摘要
本文描述了来自嗜热栖热甲烷球菌的古菌CBS结构域蛋白MJ1004的纯化及初步晶体学分析。天然蛋白经过量表达、纯化，并在单斜空间群P2(1)中结晶，晶胞参数为a = 54.4、b = 53.8、c = 82.6 Å，β = 106.1°。利用同步辐射，晶体的X射线衍射分辨率达到2.7 Å。马修斯体积计算表明，不对称单元中存在两个分子，可能对应于二聚体形式，这在溶液中也有观察到。
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