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. © 2011 International Union of Crystallography. All rights reserved.
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Kori, L. D., Hofmann, A., & Patel, B. K. C. (2011). Expression, purification and preliminary crystallographic analysis of the recombinant Β-glucosidase (BglA) from the halothermophile Halothermothrix orenii. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(1), 111–113. https://doi.org/10.1107/S1744309110046981
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