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http://purl.uniprot.org/citations/1544485http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1544485http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1544485http://www.w3.org/2000/01/rdf-schema#comment"The crystal structure of beta-lactamase TEM1 from E. coli has been solved to 2.5 A resolution by X-ray diffraction methods and refined to a crystallographic R-factor of 22.7%. The structure was determined by multiple isomorphous replacement using four heavy atom derivatives. The solution from molecular replacement, using a polyalanine model constructed from the C alpha coordinates of S. Aureus PCl enzyme, provided a set of phases used for heavy atom derivatives analysis. The E. coli beta-lactamase TEM1 is made up of two domains whose topology is similar to that of the PCl enzyme. However, global superposition of the two proteins shows significant differences."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(92)80232-6"xsd:string
http://purl.uniprot.org/citations/1544485http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(92)80232-6"xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Samama J.-P."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Samama J.-P."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Masson J.-M."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Masson J.-M."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Jelsch C."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Jelsch C."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Lenfant F."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/author"Lenfant F."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/pages"135-142"xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/pages"135-142"xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/title"Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/title"Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution."xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/volume"299"xsd:string
http://purl.uniprot.org/citations/1544485http://purl.uniprot.org/core/volume"299"xsd:string
http://purl.uniprot.org/citations/1544485http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1544485
http://purl.uniprot.org/citations/1544485http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1544485