Tanner J, Lei B, Liu M, Tu S C, Krause K L
Department of Biochemistry and Biophysical Sciences, University of Houston, TX 77204-5934.
J Mol Biol. 1994 Aug 12;241(2):283-7. doi: 10.1006/jmbi.1994.1501.
Crystals of NADPH:FMN oxidoreductase from Vibrio harveyi have been obtained and characterized by X-ray diffraction. This enzyme plays a role in the generation of light in luminescent bacteria by providing reduced FMN to luciferase. Large, high quality crystals were grown using polyethylene glycol 6000 at pH 7.0. They crystallize in the monoclinic space group P2(1) with cell dimensions a = 51.2 A, b = 85.9 A, c = 58.1 A, beta = 109.3 degrees, and diffract to 1.8 A. We expect two molecules per asymmetric unit. High resolution data sets have been recorded and a search is under way for heavy-atom derivatives.
已获得哈维氏弧菌NADPH:FMN氧化还原酶的晶体,并通过X射线衍射对其进行了表征。该酶通过为荧光素酶提供还原型FMN,在发光细菌的发光过程中发挥作用。使用聚乙二醇6000在pH 7.0条件下生长出了大尺寸、高质量的晶体。它们属于单斜晶系空间群P2(1),晶胞参数为a = 51.2 Å,b = 85.9 Å,c = 58.1 Å,β = 109.3°,衍射极限为1.8 Å。我们预计每个不对称单元中有两个分子。已记录了高分辨率数据集,目前正在寻找重原子衍生物。