Use of Patterson-based methods automatically to determine the structures of heavy-atom-containing proteins with up to 6000 non-hydrogen atoms in the asymmetric unit (Articolo in rivista)

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  • Use of Patterson-based methods automatically to determine the structures of heavy-atom-containing proteins with up to 6000 non-hydrogen atoms in the asymmetric unit (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1107/S0021889806028548 (literal)
Alternative label
  • Burla M.C. 1, Caliandro R. 2, Carrozzini B. 2, Cascarano G.L. 2, De Caro L. 2, Giacovazzo C. 2,3, Polidori G. 1, Siliqi D. 2 (2006)
    Use of Patterson-based methods automatically to determine the structures of heavy-atom-containing proteins with up to 6000 non-hydrogen atoms in the asymmetric unit
    in Journal of applied crystallography
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Burla M.C. 1, Caliandro R. 2, Carrozzini B. 2, Cascarano G.L. 2, De Caro L. 2, Giacovazzo C. 2,3, Polidori G. 1, Siliqi D. 2 (literal)
Pagina inizio
  • 728 (literal)
Pagina fine
  • 734 (literal)
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  • 39 (literal)
Rivista
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  • 7 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1 - Dip. di Science della Terra, Università di Perugia 2 - CNR-IC, Bari 3 - Dip. Geomineralogico, Università di Bari (literal)
Titolo
  • Use of Patterson-based methods automatically to determine the structures of heavy-atom-containing proteins with up to 6000 non-hydrogen atoms in the asymmetric unit (literal)
Abstract
  • The Patterson superposition methods described by Burla et al. [J. Appl. Cryst. (2006), 39, 527-535], based on the use of the `multiple implication functions', have been enriched by supplementary filtering techniques based on some general (resolution-dependent) features of both the Patterson and the electron density maps. The method has been implemented in a modified version of the program SIR2004 and tested using a set of 20 crystal structures selected from the Protein Data Bank, having a number of non-hydrogen atoms in the asymmetric unit larger than 2000, atomic resolution data and some heavy atoms (equal to or heavier than Ca). The new phasing procedure is able to solve most of the test structures, among which there are two proteins with more than 6000 non-hydrogen atoms in the asymmetric unit, so extending by far the complexity today commonly considered as the limit for Patterson-based methods (i.e. about 2000 non-hydrogen atoms). (literal)
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