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Purification, crystallization, and preliminary X‐ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes
Author(s) -
West Ann H.,
Djordjevic Snezana,
Stock Ann M.,
MartinezHackert Erik
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340210407
Subject(s) - monoclinic crystal system , chemotaxis , enzyme , crystallography , crystallization , transferase , chemistry , molecule , group (periodic table) , receptor , stereochemistry , x ray crystallography , crystal structure , diffraction , biochemistry , physics , organic chemistry , optics
Bacterial chemotaxis receptor modifying enzymes from Salmonella typhimurium have been crystallized using microseeding techniques. The crystals of the S ‐adenosyl‐ L ‐methionine‐dependent methyl transferase, CheR, belong to the monoclinic space group P 2 1 with cell constants a = 55.1 Å, b = 48.1 Å, c = 63.1 Å, β = 112.3°. The crystals of the catalytic domain of the methylesterase, CheB, belong to the trigonal space group P 3 2 21 or P 3 1 21 with unit cell dimensions of a = b = 63.4 Å, c = 86.8 Å. Both crystals contain one molecule per asymmetric unit and have calculated Matthews' volumes of 2.4 Å 3 /Da. © 1995 Wiley‐Liss, Inc.