title: Crystallization and preliminary X-ray analysis of the ytxM gene product from Bacillus subtilis.
abstract: The ytxM gene product from Bacillus subtilis has been cloned, expressed in Escherichia coli, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 3350 as the precipitant. Multiple-wavelength anomalous dispersive X-ray data have been collected to 2.0 A resolution on a single selenomethionine-incorporated crystal. This crystal belongs to the primitive orthorhombic system, with approximate unit-cell parameters a = 44.3, b = 90.9, c = 136.1 A, alpha = beta = gamma = 90 degrees and two monomers in the asymmetric unit.
authors.affiliation: The Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, England.
authors.forename: M M
authors.initials: MM
authors.lastname: Mehanni
authors.forename: A P
authors.initials: AP
authors.lastname: Turnbull
authors.forename: S E
authors.initials: SE
authors.lastname: Sedelnikova
authors.forename: P J
authors.initials: PJ
authors.lastname: Baker
authors.forename: S
authors.initials: S
authors.lastname: Foster
authors.forename: D W
authors.initials: DW
authors.lastname: Rice
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins