Wigley D B, Roper D I, Cooper R A
Department of Biochemistry, University of Leicester, U.K.
J Mol Biol. 1989 Dec 20;210(4):881-2. doi: 10.1016/0022-2836(89)90117-4.
Escherichia coli 5-carboxymethyl-2-hydroxymuconate (CHM) isomerase was purified from an overexpressing cell line. The enzyme has been crystallized from ammonium sulphate in two different crystal forms. One of these has been analysed and found to be orthorhombic I222 or I2(1)2(1)2(1) with cell dimensions a = 88 A, b = 89 A, c = 121 A. The asymmetric unit contains two dimers (Vm = 2.11 A3/dalton). The crystals diffract to beyond 3.0 A resolution and are stable to irradiation with X-rays. Data have been collected to 3.0 A resolution and a search for potential heavy-metal derivatives is in progress.
从过表达细胞系中纯化出大肠杆菌5-羧甲基-2-羟基粘康酸(CHM)异构酶。该酶已从硫酸铵中结晶出两种不同的晶体形式。其中一种已进行分析,发现为正交晶系I222或I2(1)2(1)2(1),晶胞参数a = 88 Å,b = 89 Å,c = 121 Å。不对称单元包含两个二聚体(Vm = 2.11 Å3/道尔顿)。这些晶体的衍射分辨率超过3.0 Å,并且对X射线照射稳定。已收集到3.0 Å分辨率的数据,目前正在寻找潜在的重金属衍生物。