Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes.
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.
West
A H
AH
Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Piscataway 08854, USA.
Djordjevic
S
S
Martinez-Hackert
E
E
Stock
A M
AM
D000645:Ammonium Sulfate; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification; D001483:Base Sequence; D011232:Chemical Precipitation; D002630:Chemotactic Factors / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D007477:Ions; D008780:Methyltransferases / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D012436:S-Adenosylmethionine
D001426:Bacterial Proteins; D002630:Chemotactic Factors; D007477:Ions; D012436:S-Adenosylmethionine; D008780:Methyltransferases; D000645:Ammonium Sulfate