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http://purl.uniprot.org/citations/23385463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23385463http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23385463http://www.w3.org/2000/01/rdf-schema#comment"The structure of BC0361, a polysaccharide deacetylase from Bacillus cereus, has been determined using an unconventional molecular-replacement procedure. Tens of putative models of the C-terminal domain of the protein were constructed using a multitude of homology-modelling algorithms, and these were tested for the presence of signal in molecular-replacement calculations. Of these, only the model calculated by the SAM-T08 server gave a consistent and convincing solution, but the resulting model was too inaccurate to allow phase determination to proceed to completion. The application of slow-cooling torsion-angle simulated annealing (started from a very high temperature) drastically improved this initial model to the point of allowing phasing through cycles of model building and refinement to be initiated. The structure of the protein is presented with emphasis on the presence of a C(α)-modified proline at its active site, which was modelled as an α-hydroxy-L-proline."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.org/dc/terms/identifier"doi:10.1107/S0907444912045829"xsd:string
http://purl.uniprot.org/citations/23385463http://purl.org/dc/terms/identifier"doi:10.1107/s0907444912045829"xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Bouriotis V."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Bouriotis V."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Glykos N.M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Glykos N.M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Arnaouteli S."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Arnaouteli S."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Fadouloglou V.E."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Fadouloglou V.E."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Kokkinidis M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Kokkinidis M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Agiomirgianaki A."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Agiomirgianaki A."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Kapanidou M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/author"Kapanidou M."xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/name"Acta Crystallogr D Biol Crystallogr"xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/pages"276-283"xsd:string
http://purl.uniprot.org/citations/23385463http://purl.uniprot.org/core/pages"276-283"xsd:string