Ammon H L, Murphy K C, Chandrasekhar K, Wlodawer A
J Mol Biol. 1985 Jul 5;184(1):179-81. doi: 10.1016/0022-2836(85)90051-8.
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 degrees. The crystals diffract to at least 2.2 A resolution and are suitable for X-ray crystallographic structure determination.
采用悬滴法从含硫酸铵的溶液中获得了琥珀酸弧菌L-天冬酰胺酶的晶体。这些晶体属于正交晶系空间群P22(1)2(1)，晶胞参数为a = 71.3 Å，b = 85.8 Å，c = 114.0 Å，每个晶胞包含两个四聚体酶分子。不对称单元中有两个亚基；一个分子二重轴与晶体学二重轴重合。晶体晶格与报道的大肠杆菌天冬酰胺酶的晶格相似。旋转函数计算表明，琥珀酸弧菌酶在晶体中具有222点群对称性。然而，第二个和第三个分子二重轴与相应的大肠杆菌天冬酰胺酶二重轴相差约40度。这些晶体的衍射分辨率至少为2.2 Å，适合进行X射线晶体学结构测定。
