CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF THE URACIL-DNA GLYCOSYLASE DNA-REPAIR ENZYME FROM HERPES-SIMPLEX VIRUS TYPE-1

被引：11

作者：

SAVVA, R ^{[1
]}

PEARL, LH ^{[1
]}

机构：

[1] UNIV LONDON UNIV COLL, DEPT BIOCHEM & MOLEC BIOL, BIOMOLEC STRUCT GRP, GOWER ST, LONDON WC1E 6BT, ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1993年 / 234卷 / 03期

基金：

英国惠康基金;

关键词：

CRYSTALLIZATION; HSV-1; URACIL-DNA GLYCOSYLASE; DNA REPAIR;

D O I：

10.1006/jmbi.1993.1642

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Å using a laboratory source. The enzyme crystallizes in P31 (or P32) a = 65.3 Å, c = 49.0 Å with a single molecule in the asymmetric unit and an estimated solvent content of 41% by volume. © 1993 Academic Press Limited.

引用

页码：910 / 912

页数：3

共 14 条

[1] AN AUTOMATED-SYSTEM FOR MICROBATCH PROTEIN CRYSTALLIZATION AND SCREENING [J].