CRYSTALLIZATION OF A TYPE-I 3-DEHYDROQUINASE FROM SALMONELLA-TYPHI

被引：19

作者：

BOYS, CWG

BURY, SM

SAWYER, L

MOORE, JD

CHARLES, IG

HAWKINS, AR

DEKA, R

KLEANTHOUS, C

COGGINS, JR

机构：

[1] UNIV EDINBURGH, DEPT BIOCHEM, HUGH ROBSON BLDG, GEORGE SQ, EDINBURGH EH8 9XD, SCOTLAND

[2] UNIV NEWCASTLE UPON TYNE, DEPT BIOCHEM & GENET, NEWCASTLE UPON TYNE NE2 4HH, ENGLAND

[3] WELLCOME RES LABS, DEPT EXTRATERR PHYS, BECKENHAM BR3 3BS, KENT, ENGLAND

[4] UNIV GLASGOW, DEPT BIOCHEM, GLASGOW G12 8QQ, SCOTLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1992年 / 227卷 / 01期

关键词：

3-DEHYDROQUINASE; CRYSTALLIZATION;

D O I：

10.1016/0022-2836(92)90704-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：

Crystals have been grown of a type I 3-dehydroquinase from both Escherichia coli and Salmonella typhi. However, only those from S. typhi diffract to a resolution of 2·3 Å on a conventional X-ray source and are suitable for structure determination. The space group has been determined as P21212 with unit cell dimensions a = 48·01 A ̊, b = 114·29 A ̊, c = 42·87 A ̊. There is one subunit in the asymmetric unit. © 1992.

引用

页码：352 / 355

页数：4

共 35 条

[1] A EUKARYOTIC REPRESSOR PROTEIN, THE QA-1S GENE-PRODUCT OF NEUROSPORA-CRASSA, IS HOMOLOGOUS TO PART OF THE AROM MULTIFUNCTIONAL ENZYME [J].