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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Expression, crystallization and preliminary X-ray crystallographic analysis of aldehyde dehydrogenase (ALDH) from Bacillus cereus
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Expression, crystallization and preliminary X-ray crystallographic analysis of aldehyde dehydrogenase (ALDH) from Bacillus cereus

机译:蜡状芽孢杆菌醛脱氢酶(ALDH)的表达,结晶及初步X射线晶体学分析

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摘要

Aldehyde dehydrogenase (ALDH) catalyses the oxidation of aldehydes using NAD(P)(+) as a cofactor. Most aldehydes are toxic at low levels. ALDHs are used to regulate metabolic intermediate aldehydes. The aldh gene from Bacillus cereus was cloned and the ALDH protein was expressed, purified and crystallized. A crystal of the ALDH protein diffracted to 2.6 angstrom resolution and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 83.5, b = 93.3, c = 145.5 A, beta = 98.05 degrees. Four protomers were present in the asymmetric unit, with a corresponding V-M of 2.55 angstrom(3) Da(-1) and a solvent content of 51.8%.
机译:醛脱氢酶(ALDH)使用NAD(P)(+)作为辅因子催化醛的氧化。大多数醛在低水平下是有毒的。 ALDH被用于调节代谢中间醛。克隆了蜡样芽孢杆菌的aldh基因,表达,纯化和结晶了ALDH蛋白。 ALDH蛋白的晶体衍射到2.6埃分辨率,并属于单斜晶空间群P2(1),其晶胞参数a = 83.5,b = 93.3,c = 145.5 A,β= 98.05度。在不对称单元中存在四个原型,相应的V-M为2.55埃(3)Da(-1),溶剂含量为51.8%。

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