Purification, crystallization, and preliminary X‐ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes | Zendy

West Ann H. | Zendy; Djordjevic Snezana | Zendy; Stock Ann M. | Zendy; MartinezHackert Erik | Zendy

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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.

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