Preliminary crystallographic study of an L-asparaginase from Vibrio succinogenes.
Preliminary crystallographic study of an L-asparaginase from Vibrio succinogenes.
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产琥珀酸弧菌 L-天冬酰胺酶的初步晶体学研究。
DOI：
10.1016/0022-2836(85)90051-8
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发表时间：
1985
影响因子：
5.6
通讯作者：
Wlodawer,A
中科院分区：
文献类型：
--
作者：
Ammon,HL;Murphy,KC;Chandrasekhar,K;Wlodawer,A
用挂滴法从含硫酸铵溶液中获得琥珀酸弧菌l-天冬酰胺酶结晶。晶体属于正交空间群P22 1 2 1，单位细胞尺寸为a= 71.3 a￣，b= 85.8 a￣，c= 114.0 a￣，每单位细胞含有2个四聚体酶分子。在不对称单元中有两个亚基；分子二偶与晶体二偶是一致的。晶体晶格与报道的大肠杆菌天冬酰胺酶相似。旋转函数计算表明，琥珀酸v酶在晶体中具有222点群对称性。然而，第二和第三分子对与相应的大肠杆菌天冬酰胺酶对相差约40°。该晶体的衍射分辨率至少为2.2 Å，适用于x射线晶体学结构的测定。
Crystals of an l-asparaginase from Vibrio succinogenes were obtained with the hanging drop method from ammonium sulphate-containing solutions. The crystals belong to the orthorhombic space group P22 1 2 1 with unit cell dimensions of a= 71.3 A ̊, b= 85.8 A ̊, c= 114.0 A ̊, and contain two tetrameric enzyme molecules per unit cell. There are two subunits in the asymmetric unit; a molecular dyad is coincident with the crystallographic dyad. The crystal lattice is similar to that reported for an Escherichia coli asparaginase. Rotation function calculations have revealed that the V. succinogenes enzyme has 222 point group symmetry in the crystal. The second and third molecular dyads differ, however, from the corresponding E. coli asparaginase dyads by approximately 40°. The crystals diffract to at least 2.2 Å resolution and are suitable for X-ray crystallographic structure determination.