Structural highlights
Publication Abstract from PubMed
The beta-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 A. 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.
Expression, purification and preliminary crystallographic analysis of the recombinant beta-glucosidase (BglA) from the halothermophile Halothermothrix orenii.,Kori LD, Hofmann A, Patel BK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):111-3. Epub, 2010 Dec 23. PMID:21206038[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kori LD, Hofmann A, Patel BK. Expression, purification and preliminary crystallographic analysis of the recombinant beta-glucosidase (BglA) from the halothermophile Halothermothrix orenii. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):111-3. Epub, 2010 Dec 23. PMID:21206038 doi:http://dx.doi.org/10.1107/S1744309110046981
