<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>11(7)</volume><submitter>Luang S</submitter><pubmed_abstract>Wild-type and variant crystals of a recombinant enzyme beta-d-glucan glucohydrolase from barley (Hordeum vulgare L.) were obtained by macroseeding and cross-seeding with microcrystals obtained from native plant protein. Crystals grew to dimensions of up to 500 x 250 x 375 mum at 277 K in the hanging-drops by vapour-diffusion. Further, the conditions are described that yielded the wild-type crystals with dimensions of 80 x 40 x 60 mum by self-nucleation vapour-diffusion in sitting-drops at 281 K. The wild-type and recombinant crystals prepared by seeding techniques achived full size within 5-14 days, while the wild-type crystals grown by self-nucleation appeared after 30 days and reached their maximum size after another two months. Both the wild-type and recombinant variant crystals, the la</pubmed_abstract><journal>International journal of molecular sciences</journal><pagination>2759-69</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2920565</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Crystallisation of wild-type and variant forms of a recombinant plant enzyme β-D-glucan glucohydrolase from barley (Hordeum vulgare L.) and preliminary X-ray analysis.</pubmed_title><pmcid>PMC2920565</pmcid><pubmed_authors>Streltsov VA</pubmed_authors><pubmed_authors>Ketudat Cairns JR</pubmed_authors><pubmed_authors>Hrmova M</pubmed_authors><pubmed_authors>Luang S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystallisation of wild-type and variant forms of a recombinant plant enzyme β-D-glucan glucohydrolase from barley (Hordeum vulgare L.) and preliminary X-ray analysis.</name><description>Wild-type and variant crystals of a recombinant enzyme beta-d-glucan glucohydrolase from barley (Hordeum vulgare L.) were obtained by macroseeding and cross-seeding with microcrystals obtained from native plant protein. Crystals grew to dimensions of up to 500 x 250 x 375 mum at 277 K in the hanging-drops by vapour-diffusion. Further, the conditions are described that yielded the wild-type crystals with dimensions of 80 x 40 x 60 mum by self-nucleation vapour-diffusion in sitting-drops at 281 K. The wild-type and recombinant crystals prepared by seeding techniques achived full size within 5-14 days, while the wild-type crystals grown by self-nucleation appeared after 30 days and reached their maximum size after another two months. Both the wild-type and recombinant variant crystals, the la</description><dates><release>2010-01-01T00:00:00Z</release><publication>2010 Jul</publication><modification>2025-04-18T17:02:20.109Z</modification><creation>2019-03-27T00:33:13Z</creation></dates><accession>S-EPMC2920565</accession><cross_references><pubmed>20717535</pubmed><doi>10.3390/ijms11072759</doi></cross_references></HashMap>