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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Detalles Bibliográficos
Autores principales: Morgunova, Ekaterina, Illarionov, Boris, Saller, Sabine, Popov, Aleksander, Sambaiah, Thota, Bacher, Adelbert, Cushman, Mark, Fischer, Markus, Ladenstein, Rudolf
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935281/
https://www.ncbi.nlm.nih.gov/pubmed/20823551
http://dx.doi.org/10.1107/S0907444910029690

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2935281/
https://www.ncbi.nlm.nih.gov/pubmed/20823551
http://dx.doi.org/10.1107/S0907444910029690

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