Open AccessExpression, purification and preliminary X‐ray diffraction analysis of the catalytic module of a β‐agarase from the flavobacterium Zobellia galactanivorans
Author(s) -
Hehemann JanHendrik,
Michel Gurvan,
Barbeyron Tristan,
Czjzek Mirjam
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911000429x
Subject(s) - orthorhombic crystal system , flavobacterium , polyethylene glycol , glycoside hydrolase , resolution (logic) , bacteria , chemistry , crystallography , enzyme , biology , biochemistry , crystal structure , pseudomonas , artificial intelligence , computer science , genetics
Marine bacteria secrete specific glycoside hydrolases such as agarases to access polysaccharides from algal cell walls as a carbon and energy source. In an attempt to identify agarases with variable degradation patterns, a novel family GH16 β‐agarase from the marine bacterium Zobellia galactanivorans was expressed, purified and crystallized. The purified enzyme crystallized in two distinct forms that were grown by the hanging‐drop vapour‐diffusion method using polyethylene glycol as a precipitant. Hexagonal crystals belonging to space group P 3 1 21 diffracted to 2.2 Å resolution, whereas orthorhombic crystals belonging to space group P 2 1 2 1 2 1 diffracted to 1.5 Å resolution.