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• W2039081566 abstract "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." @default.
• W2039081566 created "2016-06-24" @default.
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• W2039081566 date "1999-08-01" @default.
• W2039081566 modified "2023-09-26" @default.
• W2039081566 title "Purification, Crystallization, and Preliminary X-ray Crystallographic Analysis of Thermus thermophilus V1-ATPase B Subunit" @default.
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• W2039081566 doi "https://doi.org/10.1006/jsbi.1999.4140" @default.
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