PURIFICATION, CRYSTALLIZATION, AND PRELIMINARY-X-RAY DIFFRACTION ANALYSES OF THE BACTERIAL CHEMOTAXIS RECEPTOR MODIFYING ENZYMES

被引：13

作者：

WEST, AH

DJORDJEVIC, S

MARTINEZHACKERT, E

STOCK, AM

机构：

[1] UNIV MED & DENT NEW JERSEY,CABM,PISCATAWAY,NJ 08854

[2] UNIV MED & DENT NEW JERSEY,DEPT BIOCHEM,PISCATAWAY,NJ 08854

[3] RUTGERS STATE UNIV,DEPT CHEM,PISCATAWAY,NJ 08854

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1995年 / 21卷 / 04期

关键词：

METHYLTRANSFERASE; METHYLESTERASE; PROTEIN MODIFICATION; S-ADENOSYL-L-METHIONINE;

D O I：

10.1002/prot.340210407

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：

Bacterial chemotaxis receptor modifying enzymes from Salmonella typhimurium have been crystallized using microseeding techniques. The crystals of the S-adenosyl-L-methionine-dependent methyltransferase, CheR, belong to the monoclinic space group P2(1) with cell constants a = 55.1 Angstrom, b = 48.1 Angstrom, c = 63.1 Angstrom, beta = 112.3 degrees. The crystals of the catalytic domain of the methylesterase, CheB, belong to the trigonal space group P3(2)21 or P3(2)21 with unit cell dimensions of a = b = 63.4 Angstrom, c = 86.8 Angstrom. Both crystals contain one molecule per asymmetric unit and have calculated Matthews' volumes of 2.4 Angstrom(3)/Da. (C) 1995 Wiley-Liss, Inc.

引用

页码：345 / 350

页数：6

共 23 条

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