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Updated: Aug 19, 2026
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor
A H West1, S Djordjevic, E Martinez-Hackert
1Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Piscataway 08854, USA.
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.
