<HashMap><database>biostudies-literature</database><scores><citationCount>0</citationCount><reanalysisCount>0</reanalysisCount><viewCount>59</viewCount><searchCount>0</searchCount></scores><additional><omics_type>Unknown</omics_type><volume>62(Pt 2)</volume><submitter>Foucault M</submitter><pubmed_abstract>alpha-Galactosidases from thermophilic organisms have gained interest owing to their applications in the sugar industry. The alpha-galactosidases AgaA, AgaB and AgaA A355E mutant from Geobacillus stearothermophilus have been overexpressed in Escherichia coli. Crystals of AgaB and AgaA A355E have been obtained by the vapour-diffusion method and synchrotron data have been collected to 2.0 and 2.8 A resolution, respectively. Crystals of AgaB belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 87.5, b = 113.3, c = 161.6 A. Crystals of AgaA A355E belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 150.1, c = 233.2 A.</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>100-3</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2150962</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.</pubmed_title><pmcid>PMC2150962</pmcid><pubmed_authors>Haser R</pubmed_authors><pubmed_authors>Gouet P</pubmed_authors><pubmed_authors>Watzlawick H</pubmed_authors><pubmed_authors>Foucault M</pubmed_authors><pubmed_authors>Mattes R</pubmed_authors><view_count>59</view_count></additional><is_claimable>false</is_claimable><name>Crystallization and preliminary X-ray diffraction studies of two thermostable alpha-galactosidases from glycoside hydrolase family 36.</name><description>alpha-Galactosidases from thermophilic organisms have gained interest owing to their applications in the sugar industry. The alpha-galactosidases AgaA, AgaB and AgaA A355E mutant from Geobacillus stearothermophilus have been overexpressed in Escherichia coli. Crystals of AgaB and AgaA A355E have been obtained by the vapour-diffusion method and synchrotron data have been collected to 2.0 and 2.8 A resolution, respectively. Crystals of AgaB belong to space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 87.5, b = 113.3, c = 161.6 A. Crystals of AgaA A355E belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 150.1, c = 233.2 A.</description><dates><release>2006-01-01T00:00:00Z</release><publication>2006 Feb</publication><modification>2024-11-15T17:49:36.833Z</modification><creation>2019-03-27T02:22:16Z</creation></dates><accession>S-EPMC2150962</accession><cross_references><pubmed>16511274</pubmed><doi>10.1107/s1744309105042582</doi><doi>10.1107/S1744309105042582</doi></cross_references></HashMap>