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http://purl.uniprot.org/citations/15299314http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15299314http://www.w3.org/2000/01/rdf-schema#comment"It is often found in the crystallization of enzyme-inhibitor complexes that an inhibitor causes crystal packing which is different to that of native protein. This is the case for crystals of human non-pancreatic secreted phospholipase A(2) (124 residues) containing six molecules in the asymmetric unit when the protein is complexed with a potential acylamino analogue of a phospholid. The hexameric structure was determined by molecular replacement using the structure of monomeric native protein as a probe. As an extension to the experiment, it was tested whether a backbone polypeptide composed of 17% of a known monomeric structure could find its correct position on a target molecule in molecular replacement. A probe model composed of the backbone atoms of the N-terminal 77 residues of lysine-, arginine-, ornithine-binding protein (LAO, a total of 238 residues) liganded with lysine correctly finds its position on LAO liganded with histidine which crystallizes as a monomer in the asymmetric unit. The results indicate that as little as 17% of total diffracting matter can be used in molecular replacement to solve crystal structures or to obtain phase information which can be combined with phases obtained by the isomorphous-replacement method."xsd:string
http://purl.uniprot.org/citations/15299314http://purl.org/dc/terms/identifier"doi:10.1107/s0907444994010024"xsd:string
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/author"Oh B.H."xsd:string
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/name"Acta Crystallogr D Biol Crystallogr"xsd:string
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/pages"140-144"xsd:string
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/title"A probe molecule composed of seventeen percent of total diffracting matter gives correct solutions in molecular replacement."xsd:string
http://purl.uniprot.org/citations/15299314http://purl.uniprot.org/core/volume"51"xsd:string
http://purl.uniprot.org/citations/15299314http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15299314
http://purl.uniprot.org/citations/15299314http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15299314
http://purl.uniprot.org/uniprot/#_P14555-mappedCitation-15299314http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15299314
http://purl.uniprot.org/uniprot/P14555http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15299314