Open AccessCrystallization and preliminary crystallographic analysis of exo‐α‐1,5‐ l ‐arabinofuranosidase from Streptomyces avermitilis NBRC14893
Author(s) -
Fujimoto Zui,
Ichinose Hitomi,
Kaneko Satoshi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108029692
Subject(s) - streptomyces avermitilis , crystallization , crystallography , streptomyces , chemistry , materials science , geology , bacteria , organic chemistry , paleontology
Exo‐α‐1,5‐ l ‐arabinofuranosidase from Streptomyces avermitilis NBRC14893 (SaAraf43A) is composed of a single‐chain peptide containing a catalytic domain belonging to glycosyl hydrolase family 43 and a substrate‐binding domain belonging to carbohydrate‐binding module family 42. The enzyme catalyzes the hydrolysis of an α‐linked l ‐arabinofuranosyl residue from hemicelluloses. SaAraf43A was crystallized at 293 K using the sitting‐drop vapour‐diffusion method. The crystals belonged to space group P 2 1 2 1 2 1 and diffracted to a resolution of 2.2 Å.