Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
An intracellular beta-glucosidase (Bgl3) from Streptomyces sp. has been cloned and overexpressed in Escherichia coli. The introduction of a His tag at the N-terminal end of the protein has allowed its purification to homogeneity by a single chromatographic step, with yields of 150-200 mg of pure protein per litre of E. coli culture. The enzyme (52.6 kDa) is a retaining glycosidase able to hydrolyze a wide range of disaccharides and oligosaccharides and to perform transglycosylation. Crystals of recombinant Bgl3 have been grown from an ammonium sulfate solution using the hanging-drop vapour-diffusion method at 293 K. The crystals belong to the orthorhombic space group I222 with unit-cell dimensions a = 101.6, b = 113.4 and c = 187.5 A at room temperature and contain two molecules per asymmetric unit. A full 1.69 A resolution diffraction data set (97.7% completeness) has been collected from frozen crystals in a solution containing 30% sucrose, using synchrotron radiation.
Cloning, overexpression, crystallization and preliminary X-ray analysis of a family 1 beta--glucosidase from Streptomyces.,Guasch A, Vallmitjana M, Perez R, Querol E, Perez-Pons JA, Coll M Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):679-82. PMID:10089468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Guasch A, Vallmitjana M, Perez R, Querol E, Perez-Pons JA, Coll M. Cloning, overexpression, crystallization and preliminary X-ray analysis of a family 1 beta--glucosidase from Streptomyces. Acta Crystallogr D Biol Crystallogr. 1999 Mar;55(Pt 3):679-82. PMID:10089468
