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Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur
The highly ordered crystal structure of crambin has been solved at 1.5 Å resolution directly from the diffraction data of a native crystal at a wavelength remote from the sulphur absorption edge. The molecule has three disulphide bridges among its 46 amino acid residues, of which 46% are in helices...
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| Publié dans: | Nature |
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| Auteurs principaux: | , |
| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
1981
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5536114/ https://ncbi.nlm.nih.gov/pubmed/28769131 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/290107a0 |
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