Lee B, Yang H J, Henry G M, Seymour J P, Chibata I
J Biol Chem. 1975 Aug 25;250(16):6228-31.
Analyses of the x-ray diffraction intensity data by the Patterson synthesis and rotation function techniques show that the true space group of the monoclinic crystals of L-asparaginase (L-asparagine amidohydrolase, EC 3.5.1.1) from Proteus vulgaris is P21, that the molecular centers lie at x = 0.054, y = 0, z = 0.256, and its symmetry related positions, and that the tetramer molecules possess three approximate, mutually perpendicular 2-fold rotational symmetries, the axes of which run along the directions of the crystallographic a*-, b-, and c-axes. In addition, an investigation of the molecular packing arrangement in the crystal indicates that the tetramer molecules possess an approximately regular tetrahedral subunit structure.
通过帕特森合成法和旋转函数技术对X射线衍射强度数据进行分析表明，普通变形杆菌来源的L-天冬酰胺酶（L-天冬酰胺酰胺水解酶，EC 3.5.1.1）单斜晶体的真实空间群为P21，分子中心位于x = 0.054，y = 0，z = 0.256及其对称相关位置，并且四聚体分子具有三个近似的、相互垂直的二重旋转对称性，其轴沿晶体学a*、b和c轴方向。此外，对晶体中分子堆积排列的研究表明，四聚体分子具有近似规则的四面体亚基结构。
