Savva R, Pearl L H
Department of Biochemistry and Molecular Biology, University College London, U.K.
J Mol Biol. 1993 Dec 5;234(3):910-2. doi: 10.1006/jmbi.1993.1642.
A 28.5 kDa catalytic fragment of the uracil-DNA glycosylase DNA repair enzyme from Herpes simplex virus type 1 (HSV-1) has been crystallized using protein from a highly expressing Escherichia coli clone of the Herpes simplex virus type 1 UL2 gene. The protein crystallizes at 12 mg/ml from 11% (w/v) polyethylene glycol 8000 at pH values in the range 6.8 to 7.0, in the presence of (NH4)2SO4. Long trigonal rods (0.08 mm x 0.08 mm x > 0.5 mm) diffract beyond 3.0 A using a laboratory source. The enzyme crystallizes in P3(1) (or P3(2)) a = 65.3 A, c = 49.0 A with a single molecule in the asymmetric unit and an estimated solvent content of 41% by volume.
来自单纯疱疹病毒1型（HSV-1）的尿嘧啶-DNA糖基化酶DNA修复酶的一个28.5 kDa催化片段，已使用来自单纯疱疹病毒1型UL2基因高表达大肠杆菌克隆的蛋白质进行了结晶。该蛋白质在pH值6.8至7.0范围内，于11%（w/v）聚乙二醇8000、存在硫酸铵的条件下，以12 mg/ml的浓度结晶。使用实验室光源时，长三角棒状晶体（0.08 mm×0.08 mm×>0.5 mm）的衍射分辨率超过3.0 Å。该酶在P3(1)（或P3(2)）空间群中结晶，a = 65.3 Å，c = 49.0 Å，不对称单元中有一个单分子，估计溶剂含量为41%（体积）。
