Shibata A, Nakagawa N, Sugahara M, Masui R, Kato R, Kuramitsu S, Fukuyama K
Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan.
Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):704-5. doi: 10.1107/s0907444998015777.
A DNA excision repair enzyme, UvrB, from Thermus thermophilus HB8 was crystallized by the vapor-diffusion method using lithium sulfate as the precipitant and beta-octylglucoside as an additive. The crystals belong to the trigonal space group P3121 or P3221, with unit-cell dimensions of a = b = 136.0 and c = 108.1 A. The crystal is most likely to contain one UvrB protein in an asymmetric unit with the Vm value of 3.8 A3 Da-1. The crystals diffracted X-rays beyond 2.9 A resolution. Although the crystals were sensitive to X-ray irradiation at room temperature, the frozen crystals at 100 K showed no apparent decay during the intensity measurement.
利用硫酸锂作为沉淀剂、β-辛基葡糖苷作为添加剂，通过气相扩散法使嗜热栖热菌HB8的DNA切除修复酶UvrB结晶。晶体属于三方晶系空间群P3121或P3221，晶胞参数为a = b = 136.0 Å，c = 108.1 Å。该晶体在不对称单元中很可能含有一个UvrB蛋白，Vm值为3.8 Å3 Da-1。晶体的X射线衍射分辨率超过2.9 Å。尽管晶体在室温下对X射线照射敏感，但在100 K下冷冻的晶体在强度测量过程中未显示出明显衰减。
