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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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Detalhes bibliográficos
Publicado no:Nature
Main Authors: Hendrickson, Wayne A., Teeter, Martha M.
Formato: Artigo
Idioma:Inglês
Publicado em: 1981
Assuntos:
Acesso em linha: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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