耐辐射球菌RecR蛋白的结晶及初步X射线晶体学分析，RecR蛋白是RecFOR DNA修复途径的成员之一。
Crystallization and preliminary X-ray crystallographic analysis of the RecR protein from Deinococcus radiodurans, a member of the RecFOR DNA-repair pathway.
作者信息
Lee Byung Il, Kim Kyoung Hoon, Shim Sun Mi, Ha Kyung Soo, Yang Jin Kuk, Yoon Hye-Jin, Ha Jun Yong, Suh Se Won
机构信息
Structural Proteomics Laboratory, Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151-742, South Korea.
出版信息
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):379-81. doi: 10.1107/S0907444903028191. Epub 2004 Jan 23.
The RecR protein plays a key role in the RecFOR pathway of recombination, which is necessary for the repair of ssDNA gaps. RecR from Deinococcus radiodurans has been overexpressed in Escherichia coli and crystallized at 297 K using polyethylene glycol 1000 as a precipitant. X-ray diffraction data to 2.90 A resolution have been collected at 100 K using Cu Kalpha X-rays from a mercury-soaked crystal. The crystal belongs to space group C222(1), with unit-cell parameters a = 106.96, b = 122.25, c = 156.01 A. The asymmetric unit contains four monomers of RecR, with a crystal volume per protein weight (V(M)) of 2.57 A(3) Da(-1) and a solvent content of 51.0%.
RecR蛋白在重组的RecFOR途径中起关键作用，该途径对于单链DNA缺口的修复是必需的。来自耐辐射球菌的RecR已在大肠杆菌中过表达，并使用聚乙二醇1000作为沉淀剂在297 K下结晶。使用来自汞浸泡晶体的Cu Kα X射线在100 K下收集了分辨率为2.90 Å的X射线衍射数据。该晶体属于空间群C222(1)，晶胞参数a = 106.96、b = 122.25、c = 156.01 Å。不对称单元包含四个RecR单体，每蛋白重量的晶体体积（V(M)）为2.57 ų Da⁻¹，溶剂含量为51.0%。
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