Koike H, Sasaki H, Tanokura M, Zenno S, Saigo K
Biotechnology Research Center, University of Tokyo, Japan.
J Struct Biol. 1996 Jul-Aug;117(1):70-2. doi: 10.1006/jsbi.1996.0070.
The major flavin reductase from Vibrio fischeri, FRase I, has been crystallized in the presence of FMN by the vapor diffusion method using polyethylene glycol 4000 as a precipitant. The crystals belonged to the monoclinic space group C2 with unit cell dimensions, a = 101.6 A, b = 63.2 A, c = 74.4 A, and beta = 100.0 degrees. The crystals are expected to contain two FRase I molecules per asymmetric unit. The crystals diffracted X-rays to at least 2.2 A resolution and are appropriate for structural analysis at high resolution.
费氏弧菌的主要黄素还原酶FRase I，在黄素单核苷酸（FMN）存在的情况下，采用气相扩散法，以聚乙二醇4000作为沉淀剂进行了结晶。晶体属于单斜晶系空间群C2，晶胞参数为：a = 101.6 Å，b = 63.2 Å，c = 74.4 Å，β = 100.0°。预计每个不对称单元包含两个FRase I分子。这些晶体的X射线衍射分辨率至少达到2.2 Å，适合进行高分辨率结构分析。
