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Expression, purification and preliminary crystallographic analysis of the recombinant ?-glucosidase (BglA) from the halothermophile Halothermothrix orenii.

ABSTRACT: The ?-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.

SUBMITTER: Kori LD

PROVIDER: S-EPMC3079986 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Expression, purification and preliminary crystallographic analysis of the recombinant β-glucosidase (BglA) from the halothermophile Halothermothrix orenii.

Kori Lokesh D LD Hofmann Andreas A Patel Bharat K C BK

Acta crystallographica. Section F, Structural biology and crystallization communications 20101223 Pt 1

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. Attemp ...[more]

PMID: 21206038

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