Open AccessCrystallization and preliminary diffraction analysis of the catalytic domain of major extracellular endoglucanase from Xanthomonas campestris pv. campestris
Author(s) -
Rosseto Flávio R.,
Puhl Ana C.,
Andrade Maxuel O.,
Polikarpov Igor
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112051408
Subject(s) - cellulase , xanthomonas campestris , extracellular , hydrolase , glycoside hydrolase , chemistry , crystallization , hydrolysis , xanthomonas campestris pv. campestris , enzyme , bacteria , biochemistry , biology , organic chemistry , genetics , gene
Cellulases, such as endoglucanases, exoglucanases and β‐glucosidases, are important enzymes used in the process of enzymatic hydrolysis of plant biomass. The bacteria Xanthomonas campestris pv. campestris expresses a large number of hydrolases and the major endoglucanase (XccEG), a member of glycoside hydrolase family 5 (GH5), is the most strongly secreted extracellularly. In this work, the native XccEG was purified from the extracellular extract and crystallization assays were performed on its catalytic domain. A complete data set was collected on an in‐house X‐ray source. The crystal diffracted to 2.7 Å resolution and belonged to space group C 2, with unit‐cell parameters a = 174.66, b = 141.53, c = 108.00 Å, β = 110.49°. The Matthews coefficient suggests a solvent content of 70.1% and the presence of four protein subunits in the asymmetric unit.