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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...
| Autores principales: | , , , , , , , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
International Union of Crystallography
2010
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| Materias: | |
| 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 |