title: Crystallization of the Bacillus subtilis histidine-containing phosphocarrier protein HPr and of some of its site-directed mutants.
abstract: The histidine-containing phosphocarrier protein (HPr) from Bacillus subtilis has been crystallized. Two of the site-directed mutants aimed at probing function produce crystals suitable for X-ray studies. The mutant in which His15 is substituted by an alanyl residue crystallizes from ammonium sulfate solution in space group P3(1)21 or P3(2)21, with unit cell dimensions: a = b = 47.3 A; c = 61.5 A. These crystals diffract to at least 1.8 A resolution. The mutant in which Ser46 is substituted by an aspartyl residue crystallizes from polyethylene glycol 4000 solution in space group P2(1), with unit cell dimensions: a = 49.4 A; b = 25.6 A; c = 60.3 A; beta = 109 degrees. These crystals diffract to at least 2.0 A resolution.
authors.affiliation: Center for Advanced Research in Biotechnology, University of Maryland, Rockville 20850.
authors.forename: G
authors.initials: G
authors.lastname: Kapadia
authors.forename: J
authors.initials: J
authors.lastname: Reizer
authors.forename: S L
authors.initials: SL
authors.lastname: Sutrina
authors.forename: M H
authors.initials: MH
authors.lastname: Saier
authors.forename: P
authors.initials: P
authors.lastname: Reddy
authors.forename: O
authors.initials: O
authors.lastname: Herzberg
mesh_terms: D001412:Bacillus subtilis; D001426:Bacterial Proteins; D003460:Crystallization; D009154:Mutation; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; D011092:Polyethylene Glycols; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D011092:Polyethylene Glycols; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr