Nogi T, Fukami T A, Ishida M, Yoshida M, Miki K
Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.
J Struct Biol. 1999 Aug;127(1):79-82. doi: 10.1006/jsbi.1999.4140.
The gene of V(1)-ATPase B subunit from the thermophilic eubacterium Thermus thermophilus has been cloned and the protein overproduced in Escherichia coli. The purified protein, with a molecular weight of 53.2 kDa, was crystallized from 10% (w/v) polyethylene glycol 1000, 120 mM magnesium chloride, and 100 mM Na-tricine, pH 8.0, by the vapor diffusion method. The crystals diffracted X-rays beyond 3.5 A on a synchrotron radiation source. The crystals belong to the monoclinic space group C2, with unit cell dimensions of a = 153.1 A, b = 129.6 A, c = 92.7 A, and beta = 100.3 degrees. Assuming that three or four molecules are contained in an asymmetric unit, the V(M) value is calculated as 2.8 or 2.1 A (3)/Da, respectively.
嗜热真细菌嗜热栖热菌（Thermus thermophilus）的V(1)-ATP酶B亚基基因已被克隆，并在大肠杆菌中过量表达了该蛋白。纯化后的蛋白分子量为53.2 kDa，通过气相扩散法，从含有10%（w/v）聚乙二醇1000、120 mM氯化镁和100 mM Na-三（羟甲基）甲基甘氨酸（pH 8.0）的溶液中结晶。这些晶体在同步辐射源上的X射线衍射分辨率超过3.5 Å。晶体属于单斜空间群C2，晶胞参数为a = 153.1 Å，b = 129.6 Å，c = 92.7 Å，β = 100.3°。假设一个不对称单位中包含三个或四个分子，则V(M)值分别计算为2.8或2.1 Å(3)/Da。
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