Abstract
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 and 17% are in a β-sheet. Crambin is shown to be an amphipathic protein, inasmuch as its six charged groups are segregated from hydrophobic surface elements. Phasing methods used here will also apply elsewhere.
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Hendrickson, W., Teeter, M. Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature 290, 107–113 (1981). https://doi.org/10.1038/290107a0
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DOI: https://doi.org/10.1038/290107a0
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