噬菌体T4嘧啶二聚体特异性切除修复酶的初步晶体学研究。

Preliminary crystallographic study of pyrimidine dimer-specific excision-repair enzyme from bacteriophage T4.

作者信息

Morikawa K, Tsujimoto M, Ikehara M, Inaoka T, Ohtsuka E

机构信息

Protein Engineering Research Institute, Tokyo, Japan.

出版信息

J Mol Biol. 1988 Aug 5;202(3):683-4. doi: 10.1016/0022-2836(88)90298-7.

DOI:10.1016/0022-2836(88)90298-7

PMID:3172233

Abstract

Bacteriophage T4 endonuclease V, which is an excision-repair enzyme specific to pyrimidine dimers within DNA, has been crystallized from polyethylene glycol 4000 solution by a vapour diffusion technique. The unit cell is monoclinic, space group P2(1), with unit cell parameters: a = 41.4 A, b = 40.1 A, c = 37.5 A, beta = 90.01 degrees. The unit cell contains two 16,000 Mr molecules. The crystals diffract X-rays beyond 2.3 A resolution and are suitable for structural analysis at high resolution.

摘要

噬菌体T4内切核酸酶V是一种对DNA中的嘧啶二聚体具有特异性的切除修复酶，已通过气相扩散技术从聚乙二醇4000溶液中结晶出来。晶胞为单斜晶系，空间群为P2(1)，晶胞参数为：a = 41.4 Å，b = 40.1 Å，c = 37.5 Å，β = 90.01°。晶胞包含两个16,000相对分子质量的分子。这些晶体的X射线衍射分辨率超过2.3 Å，适合进行高分辨率结构分析。