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http://purl.uniprot.org/citations/18678936http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18678936http://www.w3.org/2000/01/rdf-schema#comment"The decameric inducible lysine decarboxylase (LdcI) from Escherichia coli has been crystallized in space groups C2 and C222(1); the Ta6Br12(2+) cluster was used to derivatize the C2 crystals. The method of single isomorphous replacement with anomalous scattering (SIRAS) as implemented in SHELXD was used to solve the Ta6Br12(2+)-derivatized structure to 5 A resolution. Many of the Ta6Br12(2+)-binding sites had twofold and fivefold noncrystallographic symmetry. Taking advantage of this feature, phase modification was performed in DM. The electron-density map of LdcI displays many features in agreement with the low-resolution negative-stain electron-density map [Snider et al. (2006), J. Biol. Chem. 281, 1532-1546]."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.org/dc/terms/identifier"doi:10.1107/s1744309108018757"xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/author"Pai E.F."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/author"Snider J."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/author"Kanjee U."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/author"Houry W.A."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/author"Alexopoulos E."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/name"Acta Crystallogr Sect F Struct Biol Cryst Commun"xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/pages"700-706"xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/title"Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/18678936http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/18678936http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18678936
http://purl.uniprot.org/citations/18678936http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18678936
http://purl.uniprot.org/uniprot/#_P0A9H3-mappedCitation-18678936http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18678936
http://purl.uniprot.org/uniprot/P0A9H3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18678936