Crystallization and preliminary X-ray analysis of family 39 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 crystallization and preliminary X-ray analysis of the beta-D-xylosidase (XynB1) from Geobacillus stearothermophilus T-6, a family 39 glycoside hydrolase, are described. XynB1 is a tetrameric protein consisting of four identical subunits of 503 amino acids and with a calculated molecular weight of 58 001 Da. Both the native and the selenomethionine-containing XynB1 were crystallized by the hanging-drop vapour-diffusion method and the crystals were found to belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 92.7, b = 165.7, c = 311.0 A. The native crystals diffracted X-rays to a resolution of 2.1 A.
Architecture et Fonction des Macromolécules Biologiques, CNRS-Université de Provence, Université d'Aix-Marseille II, IBSM, 31 Chemin Joseph-Aiguier, 13402 Marseille CEDEX 20, France. czjzek@afmb.cnrs-mrs.fr
Mirjam
M
Czjzek
Tsafrir
T
Bravman
Bernard
B
Henrissat
Yuval
Y
Shoham
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry* / Q000378:metabolism; D045302:Geobacter / Q000201:enzymology* / Q000378:metabolism; D009844:Oligosaccharides / Q000378:metabolism; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D012645:Selenomethionine / Q000737:chemistry; D014994:Xylose / Q000378:metabolism; D001617:beta-Glucosidase / Q000737:chemistry* / Q000378:metabolism
D001426:Bacterial Proteins; D009844:Oligosaccharides; D021122:Protein Subunits; D012645:Selenomethionine; D014994:Xylose; D001617:beta-Glucosidase; D043364:Endo-1,4-beta Xylanases; C090001:XynB xylanase