大鼠DNA聚合酶β 31 kDa C端片段的结晶

Crystallization of 31 kDa C-terminal fragment of rat DNA polymerase beta.

作者信息

Shirakihara Y, Matsukage A, Nishimoto Y, Date T

机构信息

Department of Physics, Hyogo University of Education, Japan.

出版信息

J Mol Biol. 1994 Jan 28;235(4):1342-4. doi: 10.1006/jmbi.1994.1087.

DOI:10.1006/jmbi.1994.1087

PMID:8308896

Abstract

A 248 residue C-terminal fragment of rat DNA polymerase beta (335 amino acid residues), a eukaryotic DNA repair enzyme, has been crystallized from polyethylene glycol 6000 solution. The crystals are orthorhombic, space group P2(1)2(1)2 with cell dimensions a = 120.3 A, b = 64.2 A, c = 39.4 A, and contain a single 31 kDa fragment in an asymmetric unit. The crystals diffract to 2.8 A resolution with laboratory X-ray source, and to 2.3 A resolution with synchrotron X-ray source, and are suitable for detailed structural analysis.

摘要

大鼠DNA聚合酶β（335个氨基酸残基）的一个248个残基的C末端片段，一种真核生物DNA修复酶，已从聚乙二醇6000溶液中结晶出来。晶体为正交晶系，空间群P2(1)2(1)2，晶胞参数a = 120.3 Å，b = 64.2 Å，c = 39.4 Å，在不对称单元中包含一个单一的31 kDa片段。这些晶体用实验室X射线源可衍射到2.8 Å分辨率，用同步加速器X射线源可衍射到2.3 Å分辨率，适合进行详细的结构分析。