<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>66(Pt 4)</volume><submitter>Hehemann JH</submitter><pubmed_abstract>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 beta-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 P3(1)21 diffracted to 2.2 A resolution, whereas orthorhombic crystals belonging to space group P2(1)2(1)2(1) diffracted to 1.5 A resolution.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>413-7</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2852333</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Expression, purification and preliminary X-ray diffraction analysis of the catalytic module of a beta-agarase from the flavobacterium Zobellia galactanivorans.</pubmed_title><pmcid>PMC2852333</pmcid><pubmed_authors>Barbeyron T</pubmed_authors><pubmed_authors>Czjzek M</pubmed_authors><pubmed_authors>Hehemann JH</pubmed_authors><pubmed_authors>Michel G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Expression, purification and preliminary X-ray diffraction analysis of the catalytic module of a beta-agarase from the flavobacterium Zobellia galactanivorans.</name><description>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 beta-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 P3(1)21 diffracted to 2.2 A resolution, whereas orthorhombic crystals belonging to space group P2(1)2(1)2(1) diffracted to 1.5 A resolution.</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Apr</publication><modification>2026-05-01T15:52:17.041Z</modification><creation>2026-04-07T17:04:22.667Z</creation></dates><accession>S-EPMC2852333</accession><cross_references><pubmed>20383011</pubmed><doi>10.1107/s174430911000429x</doi><doi>10.1107/S174430911000429X</doi></cross_references></HashMap>