Open AccessCrystallization and preliminary X‐ray crystallographic studies of XynX, a family 10 xylanase from Aeromonas punctata ME‐1
Author(s) -
Fujimoto Zui,
Usui Kengo,
Kondo Yukari,
Yasui Kazumasa,
Kawai Keiichi,
Suzuki Tohru
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105002058
Subject(s) - xylobiose , orthorhombic crystal system , xylanase , glycoside hydrolase , crystallography , misorientation , xylan , crystallization , cellobiose , chemistry , hydrolysis , glycosidic bond , resolution (logic) , stereochemistry , enzyme , biochemistry , crystal structure , organic chemistry , cellulase , microstructure , artificial intelligence , computer science , grain boundary
Xylanases catalyze the hydrolysis of β‐1,4‐glycosidic linkages within the xylan backbone. XynX is a xylanase from Aeromonas punctata ME‐1 and belongs to glycoside hydrolase family 10. While most xylanases show endo‐type catalytic activities, XynX shows exo‐like catalytic activities, selectively producing xylobiose from birchwood xylan. In this study, XynX was crystallized by the hanging‐drop vapour‐diffusion method. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 79.0, b = 88.6, c = 93.2 Å, and diffracted to beyond 1.8 Å resolution.