title: Expression, purification and preliminary crystallographic analysis of the recombinant β-glucosidase (BglA) from the halothermophile Halothermothrix orenii.
abstract: The β-glucosidase A gene (bglA) has been cloned from the halothermophilic bacterium Halothermothrix orenii and the recombinant enzyme (BglA; EC 3.2.1.21) was bacterially expressed, purified using metal ion-affinity chromatography and subsequently crystallized. Orthorhombic crystals were obtained that diffracted to a resolution limit of 3.5 Å. The crystal structure with two molecules in the asymmetric unit was solved by molecular replacement using a library of known glucosidase structures. Attempts to collect higher resolution diffraction data from crystals grown under different conditions and structure refinement are currently in progress.
authors.affiliation: Microbial Gene Research and Resources Facility, School of Biomolecular and Physical Sciences, Griffith University, Brisbane QLD 4111, Australia.
authors.forename: Lokesh D
authors.initials: LD
authors.lastname: Kori
authors.forename: Andreas
authors.initials: A
authors.lastname: Hofmann
authors.forename: Bharat K C
authors.initials: BK
authors.lastname: Patel
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D001617:beta-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D011994:Recombinant Proteins; D001617:beta-Glucosidase