仙茅甜蛋白的结晶及初步X射线衍射研究。一种具有味觉修饰作用的新型甜味蛋白。
Crystallization and preliminary X-ray diffraction studies of curculin. A new type of sweet protein having taste-modifying action.
作者信息
Harada S, Otani H, Maeda S, Kai Y, Kasai N, Kurihara Y
机构信息
Department of Applied Chemistry, Faculty of Engineering Osaka University, Japan.
出版信息
J Mol Biol. 1994 Apr 29;238(2):286-7. doi: 10.1006/jmbi.1994.1289.
PMID:8158656
Abstract
A taste-modifying protein, curculin, has been crystallized by the vapor diffusion method using polyethylene glycol 400 as a precipitant. The crystals belong to orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions: a = 105 A, b = 271 A, c = 48.7 A. The crystals diffract X-rays to at least a resolution of 3.0 A and are suitable for X-ray crystallographic studies.
摘要
一种味觉修饰蛋白——仙茅蛋白，已通过气相扩散法，以聚乙二醇400作为沉淀剂进行了结晶。晶体属于正交晶系空间群P2(1)2(1)2(1)，晶胞参数为：a = 105 Å，b = 271 Å，c = 48.7 Å。这些晶体对X射线的衍射分辨率至少为3.0 Å，适用于X射线晶体学研究。
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