Abstract
The chemotaxis histidine kinase CheA assembles into a dimer in which the P3 dimerization domain forms a four-helix bundle by the parallel association of two α-helical hairpins from each subunit. Ligand occupancy of the chemoreceptor regulates signal transduction by controlling the autophosphorylation activity of CheA. Autophosphorylation of CheA occurs in trans, i.e. one subunit phosphorylates the other. The P3 domain of CheA from Escherichia coli has been overexpressed in E. coli and crystallized at 298 K using PEG as a precipitant. X-ray diffraction data to 2.80 Å resolution have been collected at 100 K using synchrotron radiation. The crystal belonged to space group P1, with unit-cell parameters a = 59.271, b = 67.674, c = 82.815 Å, α = 77.568, β = 86.073, γ = 64.436°. The asymmetric unit may contain up to ten dimeric units of P3 four-helix bundles.