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Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases.
A new conformational database potential involving dihedral angle relationships in databases of high-resolution highly refined protein crystal structures is presented as a method for improving the quality of structures generated from NMR data. The rationale for this procedure is based on the observat...
Gardado en:
| Main Authors: | , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
1996
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143426/ https://ncbi.nlm.nih.gov/pubmed/8762138 |
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