Open AccessCrystallization and preliminary X‐ray crystallographic analysis of BxlA, an intracellular β‐ d ‐xylosidase from Streptomyces thermoviolaceus OPC‐520
Author(s) -
Morioka Hideaki,
Miki Yasuhiro,
Saito Kei,
Tomoo Koji,
Ishida Toshimasa,
Hasegawa Tomokazu,
Yamano Akihito,
Takada Chiaki,
Miyamoto Katsushiro,
Tsujibo Hiroshi
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110013400
Subject(s) - crystallization , crystallography , monoclinic crystal system , intracellular , chemistry , extracellular , molecule , crystal structure , biochemistry , organic chemistry
BxlA from Streptomyces thermoviolaceus OPC‐520, together with the extracellular BxlE and the integral membrane proteins BxlF and BxlG, constitutes a xylanolytic system that participates in the intracellular transport of xylan‐degradation products and the production of xylose. To elucidate the mechanism of the hydrolytic degradation of xylooligosaccharides to xylose at the atomic level, X‐ray structural analysis of BxlA was attempted. The recombinant BxlA protein (molecular weight 82 kDa) was crystallized by the hanging‐drop vapour‐diffusion method at 289 K. The crystals belonged to the monoclinic space group C 2, with unit‐cell parameters a = 142.2, b = 129.5, c = 101.4 Å, β = 119.8°, and contained two molecules per asymmetric unit ( V M = 2.47 Å 3 Da −1 ). Diffraction data were collected to a resolution to 2.50 Å and provided a data set with an overall R merge of 8.3%.