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Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis

The crystal structure of lumazine synthase from Bacillus anthracis was solved by molecular replacement and refined to R (cryst) = 23.7% (R (free) = 28.4%) at a resolution of 3.5 Å. The structure reveals the icosahedral symmetry of the enzyme and specific features of the active site that are unique i...

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Detalhes bibliográficos
Main Authors: Morgunova, Ekaterina, Illarionov, Boris, Saller, Sabine, Popov, Aleksander, Sambaiah, Thota, Bacher, Adelbert, Cushman, Mark, Fischer, Markus, Ladenstein, Rudolf
Formato: Artigo
Idioma:Inglês
Publicado em: International Union of Crystallography 2010
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2935281/
https://ncbi.nlm.nih.gov/pubmed/20823551
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S0907444910029690
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