Overexpression, purification, crystallization and preliminary crystallographic studies on a thermostable beta-glycosidase from Thermus nonproteolyticus HG102

Authors
He, XY Wang, XQ Yang, SJ Chang, WR Liang, DC
Citation
Xy. He et al., Overexpression, purification, crystallization and preliminary crystallographic studies on a thermostable beta-glycosidase from Thermus nonproteolyticus HG102, ACT CRYST D, 57, 2001, pp. 1650-1651
Citations number
23
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
11
Pages
1650 - 1651
Database
ISI
SICI code
0907-4449(200111)57:<1650:OPCAPC>2.0.ZU;2-H
Abstract
A thermostable beta -glycosidase (Tn-gly) from Thermus nonproteolyticus HG1 02 has been cloned and overexpressed in Escherichia coli. The recombinant e nzyme, with a molecular mass of 48.9 kDa, was purified to homogeneity. It c an hydrolyze a wide range of oligosaccharides and perform transglycosylatio n. Crystals of the recombinant enzyme were grown by the hanging-drop vapour -diffusion technique with MPD and NaCl as precipitants. They belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 66.7, b = 94.6, c = 176.5 Angstrom.