Overexpression, purification, crystallization and preliminary crystallographic studies on a thermostable beta-glycosidase from Thermus nonproteolyticus HG102.
A thermostable beta-glycosidase (Tn-gly) from Thermus nonproteolyticus HG102 has been cloned and overexpressed in Escherichia coli. The recombinant enzyme, with a molecular mass of 48.9 kDa, was purified to homogeneity. It can hydrolyze a wide range of oligosaccharides and perform transglycosylation. 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 A.
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Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, People's Republic of China.
Wang
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XQ
Yang
S J
SJ
Chang
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WR
Liang
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DC
D003460:Crystallization; D018360:Crystallography, X-Ray; D006026:Glycoside Hydrolases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013824:Thermus / Q000201:enzymology*; D001617:beta-Glucosidase
D006026:Glycoside Hydrolases; D001617:beta-Glucosidase; C441633:beta-glycosidase, Thermus nonproteolyticus