<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>64(Pt 2)</volume><submitter>Kurz M</submitter><pubmed_abstract>alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The alpha-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet alpha-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 A, beta = 107.0 degrees and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 A using a copper anode and data from SeMet alpha-DsbA1 crystals wer</pubmed_abstract><journal>Acta crystallographica. Section F, Structural biology and crystallization communications</journal><pagination>94-7</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2374166</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.</pubmed_title><pmcid>PMC2374166</pmcid><pubmed_authors>Jarrott R</pubmed_authors><pubmed_authors>Iturbe-Ormaetxe I</pubmed_authors><pubmed_authors>O'Neill SL</pubmed_authors><pubmed_authors>Byriel KA</pubmed_authors><pubmed_authors>Heras B</pubmed_authors><pubmed_authors>Martin JL</pubmed_authors><pubmed_authors>Kurz M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia pipientis.</name><description>alpha-DsbA1 is one of two DsbA homologues encoded by the Gram-negative alpha-proteobacterium Wolbachia pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The alpha-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet alpha-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 A, beta = 107.0 degrees and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 A using a copper anode and data from SeMet alpha-DsbA1 crystals wer</description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Feb</publication><modification>2025-04-21T18:05:50.586Z</modification><creation>2019-03-27T00:13:56Z</creation></dates><accession>S-EPMC2374166</accession><cross_references><pubmed>18259058</pubmed><doi>10.1107/S1744309108000055</doi><doi>10.1107/s1744309108000055</doi></cross_references></HashMap>