title: Cloning, purification and crystallographic analysis of a hypothetical protein, BPSL1549, from Burkholderia pseudomallei.
abstract: Burkholderia pseudomallei BPSL1549, a putative protein of unknown function, has been overexpressed in Escherichia coli, purified and subsequently crystallized by the hanging-drop vapour-diffusion method using PEG as a precipitant to give crystals with overall dimensions of 0.15 × 0.15 × 0.1 mm. Native data were collected to 1.47 Å resolution at the European Synchrotron Radiation Facility (ESRF). The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.1, b = 45.4, c = 111.9 Å and with a single polypeptide chain in the asymmetric unit.
authors.affiliation: Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield, England.
authors.forename: Abimael
authors.initials: A
authors.lastname: Cruz-Migoni
authors.forename: Sergey N
authors.initials: SN
authors.lastname: Ruzheinikov
authors.forename: Svetlana E
authors.initials: SE
authors.lastname: Sedelnikova
authors.forename: Barbara
authors.initials: B
authors.lastname: Obeng
authors.forename: Sylvia
authors.initials: S
authors.lastname: Chieng
authors.forename: Rahmah
authors.initials: R
authors.lastname: Mohamed
authors.forename: Sheila
authors.initials: S
authors.lastname: Nathan
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Baker
authors.forename: David W
authors.initials: DW
authors.lastname: Rice
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D016957:Burkholderia pseudomallei / Q000737:chemistry*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray
chemical_list: D001426:Bacterial Proteins