Open AccessPurification, 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.