Open AccessCrystallization and preliminary X‐ray analysis of α‐xylosidase from Escherichia coli
Author(s) -
Kitamura Momoyo,
Ose Toyoyuki,
Okuyama Masayuki,
Watanabe Hiromi,
Yao Min,
Mori Haruhide,
Kimura Atsuo,
Tanaka Isao
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104033202
Subject(s) - escherichia coli , glycoside hydrolase , xylose , crystallization , chemistry , crystallography , glycoside , molecule , stereochemistry , x ray crystallography , diffraction , fermentation , enzyme , biochemistry , organic chemistry , physics , gene , optics
Glycoside hydrolases have been implicated in many biological processes. To date, they have been classified into 93 glycoside hydrolase (GH) families based on amino‐acid sequence similarity. α‐Xylosidase from Escherichia coli belongs to GH family 31 and catalyzes the release of α‐xylose from the non‐reducing terminal side of α‐xyloside. Single crystals of α‐xylosidase have been grown by vapour diffusion at 293 K from 10%( w / v ) PEG 20K, 2%( v / v ) 2‐propanol, 2%( v / v ) glycerol and 0.1 M 2‐morpholinoethanesulfonic acid pH 5.5. These crystals belong to space group P 2 1 2 1 2 1 and X‐ray diffraction data were collected to a resolution of 2.75 Å. Crystals of selenomethionyl‐substituted α‐xylosidase were also obtained, which diffracted to at least 3.0 Å. Based on the value of V M , the asymmetric unit in these crystals was assumed to contain six molecules.