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Updated: Jun 5, 2026
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Expression, purification and preliminary crystallographic analysis of the recombinant β-glucosidase (BglA) from the
Lokesh D Kori1, Andreas Hofmann, Bharat K C Patel
1Microbial Gene Research and Resources Facility, School of Biomolecular and Physical Sciences, Griffith University, Brisbane QLD 4111, Australia.
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.
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