细菌趋化性受体修饰酶的纯化、结晶及初步X射线衍射分析。

Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.

作者信息

West A H, Djordjevic S, Martinez-Hackert E, Stock A M

机构信息

Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Piscataway 08854, USA.

出版信息

Proteins. 1995 Apr;21(4):345-50. doi: 10.1002/prot.340210407.

DOI:10.1002/prot.340210407

PMID:7567955

Abstract

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 P21 with cell constants a = 55.1 A, b = 48.1 A, c = 63.1 A, 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(1)21 with unit cell dimensions of a = b = 63.4 A, c = 86.8 A. Both crystals contain one molecule per asymmetric unit and have calculated Matthews' volumes of 2.4 A3/Da.

摘要

利用微种晶技术已使鼠伤寒沙门氏菌的细菌趋化性受体修饰酶结晶。依赖S-腺苷-L-甲硫氨酸的甲基转移酶CheR的晶体属于单斜空间群P21，晶胞参数为a = 55.1 Å，b = 48.1 Å，c = 63.1 Å，β = 112.3°。甲基酯酶CheB催化结构域的晶体属于三方空间群P3(2)21或P3(1)21，晶胞尺寸为a = b = 63.4 Å，c = 86.8 Å。两种晶体的不对称单元均包含一个分子，计算得到的马修斯体积为2.4 Å³/Da。