CRYSTALLIZATION OF HUMAN THYMIDYLATE SYNTHASE

被引：11

作者：

SCHIFFER, CA

DAVISSON, VJ

SANTI, DV

STROUD, RM

机构：

[1] UNIV CALIF SAN FRANCISCO,DEPT BIOCHEM & BIOPHYS,SAN FRANCISCO,CA 94143

[2] UNIV CALIF SAN FRANCISCO,GRAD GRP BIOPHYS,SAN FRANCISCO,CA 94143

[3] UNIV CALIF SAN FRANCISCO,DEPT PHARMACEUT CHEM,SAN FRANCISCO,CA 94143

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1991年 / 219卷 / 02期

关键词：

THYMIDYLATE SYNTHASE; CRYSTALLOGRAPHY; ENZYME; PROTEIN STRUCTURE; CANCER;

D O I：

10.1016/0022-2836(91)90558-N

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：

Human thymidylate synthase has been crystallized in the absence of ligands and diffracts beyond 3.0 Å. The protein was cloned and expressed in Escherichia coli and then crystallized from ammonium sulfate in the presence of β-mercaptoethanol at a variety of pH values. The crystals are trigonal in the space-group P3121; the unit cell dimensions are a = b = 96·7 A ̊, c = 84·1 A ̊. © 1991.

引用

页码：161 / 163

页数：3

共 11 条

[1] A SYSTEM FOR COLLECTION AND ONLINE INTEGRATION OF X-RAY-DIFFRACTION DATA FROM A MULTIWIRE AREA DETECTOR [J].