Open AccessCrystallization and preliminary crystallographic analysis of β‐ l ‐arabinopyranosidase from Streptomyces avermitilis NBRC14893
Author(s) -
Fujimoto Zui,
Ichinose Hitomi,
Harazono Koichi,
Honda Mariko,
Uzura Atsuko,
Kaneko Satoshi
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109017230
Subject(s) - streptomyces avermitilis , crystallization , crystallography , streptomyces , monomer , chemistry , glycosyl , stereochemistry , materials science , biology , polymer , bacteria , organic chemistry , genetics
β‐ l ‐Arabinopyranosidase from Streptomyces avermitilis NBRC14893 is a monomeric protein consisting of a catalytic domain belonging to glycosyl hydrolase family 27, an unknown domain and a substrate‐binding domain belonging to carbohydrate‐binding module family 13. The complete enzyme (residues 45–658) has successfully been cloned and homologously expressed in the Streptomyces expression system. β‐ l ‐Arabinopyranosidase was crystallized by the sitting‐drop vapour‐diffusion method. The crystals diffracted to 1.6 Å resolution and belonged to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 68.2, b = 98.9, c = 181.3 Å. The Matthews coefficient was calculated to be 2.38 Å 3 Da −1 .