Crystallization and preliminary crystallographic analysis of a thermostable family 52 beta-D-xylosidase from Geobacillus stearothermophilus T-6.
Beta-D-xylosidases (EC 3.2.1.37) are hemicellulases that hydrolyze short xylooligosaccharides into single xylose units. In this study, the first crystallization and preliminary X-ray analysis of a family 52 glycoside hydrolase, the beta-D-xylosidase (XynB2) from Geobacillus stearothermophilus T-6, is described. XynB2 is a dimeric protein consisting of two identical subunits of 705 amino acids with a calculated molecular weight of 79 894 Da. XynB2 was crystallized by the hanging-drop vapour-diffusion method and the crystals were found to belong to space group P1, with unit-cell parameters a = 80.6, b = 97.5, c = 107.2 A, alpha = 107.4, beta = 98.2, gamma = 106.6 degrees. The native crystals diffracted X-rays to a resolution of 2.0 A.
Architecture et Fonction des Macromolécules Biologiques, CNRS-Université de Provence-Université d'Aix-Marseille II, UMR 6098, 31 Chemin Joseph Aiguier, 13402 CEDEX 20, France. czjzek@afmb.cnrs-mrs.fr
Mirjam
M
Czjzek
Tsafrir
T
Bravman
Bernard
B
Henrissat
Yuval
Y
Shoham
D001406:Bacillaceae / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D006358:Hot Temperature; D014995:Xylosidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D014995:Xylosidases