title: Crystallization and preliminary X-ray analysis of the controller protein C.AhdI from Aeromonas hydrophilia.
abstract: Single crystals of purified homodimeric controller protein from Aeromonas hydrophilia (C.AhdI) have been grown under several different conditions using vapour diffusion. X-ray diffraction data have been collected using synchrotron radiation from crystals of both the native and a selenomethionine (SeMet) derivative of the protein. The native crystal form belongs to space group P2(1) and data were collected to a resolution of 2.2 A. Two crystal forms of the SeMet protein have been obtained and were found to belong to space groups P1 and P2(1); data have been recorded to 2.0 and 1.7 A resolution, respectively, for the two crystal forms. Three-wavelength MAD data were collected to 1.7 A for the SeMet derivative crystal, which is isomorphous with the native P2(1) crystal.
authors.affiliation: Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, University of Portsmouth, Portsmouth PO1 2DT, England.
authors.forename: J E
authors.initials: JE
authors.lastname: McGeehan
authors.forename: S
authors.initials: S
authors.lastname: Streeter
authors.forename: J B
authors.initials: JB
authors.lastname: Cooper
authors.forename: F
authors.initials: F
authors.lastname: Mohammed
authors.forename: G C
authors.initials: GC
authors.lastname: Fox
authors.forename: G G
authors.initials: GG
authors.lastname: Kneale
mesh_terms: D000333:Aeromonas / Q000378:metabolism*; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D012542:Scattering, Radiation; D012645:Selenomethionine / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D011994:Recombinant Proteins; D012645:Selenomethionine