Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur.
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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.
SUBMITTER: Hendrickson WA
PROVIDER: S-EPMC5536114 | biostudies-other | 1981 Mar
REPOSITORIES: biostudies-other
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