Purification, crystallization and preliminary X‐ray analysis of a thermostable glycoside hydrolase family 43 β‐xylosidase from  Geobacillus thermoleovorans  IT‐08
Author(s) - 
Rohman Ali, 
Van Oosterwijk Niels, 
Kralj Slavko, 
Dijkhuizen Lubbert, 
Dijkstra Bauke W., 
Puspaningsih Ni Nyoman Tri
Publication year - 2007
Publication title - 
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107046015
Subject(s) - xylanase , thermophile , chemistry , glycoside hydrolase , hydrolysis , crystallization , geobacillus stearothermophilus , crystallography , orthorhombic crystal system , xylose , enzyme , stereochemistry , crystal structure , biochemistry , organic chemistry , fermentation
The main enzymes involved in xylan‐backbone hydrolysis are endo‐1,4‐β‐xylanase and β‐xylosidase. β‐Xylosidase converts the xylo‐oligosaccharides produced by endo‐1,4‐β‐xylanase into xylose monomers. The β‐xylosidase from the thermophilic  Geobacillus thermoleovorans  IT‐08, a member of glycoside hydrolase family 43, was crystallized at room temperature using the hanging‐drop vapour‐diffusion method. Two crystal forms were observed. Bipyramid‐shaped crystals belonging to space group  P 4 3 2 1 2, with unit‐cell parameters  a  =  b  = 62.53,  c  = 277.4 Å diffracted to 1.55 Å resolution. The rectangular crystals belonged to space group  P 2 1 , with unit‐cell parameters  a  = 57.94,  b  = 142.1,  c  = 153.9 Å, β = 90.5°, and diffracted to 1.80 Å resolution.
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