大肠杆菌镍结合蛋白NikA的结晶及初步X射线衍射研究
Crystallization and preliminary X-ray diffraction study of the nickel-binding protein NikA of Escherichia coli.
作者信息
Charon M H, Wu L F, Piras C, de Pina K, Mandrand-Berthelot M A, Fontecilla-Camps J C
机构信息
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale J. P. Ebel CEA-CNRS, Grenoble, France.
出版信息
J Mol Biol. 1994 Oct 21;243(2):353-5. doi: 10.1006/jmbi.1994.1661.
NikA, a periplasmic nickel-binding protein involved in nickel-repellent chemotaxis has been crystallized. The crystals are hexagonal with space group P6(2) (or its enantiomorph) with a = 160.3 A and c = 138.4 A and they diffract to at least 3.0 A resolution in the laboratory. NikA presents sequence homology with several periplasmic solute-binding proteins from Gram-negative bacteria.
NikA是一种参与镍排斥趋化作用的周质镍结合蛋白，现已结晶。晶体为六方晶系，空间群为P6(2)（或其对映体），a = 160.3 Å，c = 138.4 Å，在实验室中其衍射分辨率至少为3.0 Å。NikA与几种革兰氏阴性菌的周质溶质结合蛋白存在序列同源性。
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