Open AccessExpression, purification and preliminary crystallographic analysis of the recombinant β‐glucosidase (BglA) from the halothermophile Halothermothrix orenii
Author(s) -
Kori Lokesh D.,
Hofmann Andreas,
Patel Bharat K. C.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110046981
Subject(s) - recombinant dna , orthorhombic crystal system , molecular replacement , resolution (logic) , chemistry , molecule , enzyme , crystal structure , chromatography , crystallography , biochemistry , gene , organic chemistry , artificial intelligence , computer science
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.