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10.1038/290107a0

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C5536114!5536114 !28769131
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suck abstract from ncbi


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pmid28769131
      Nature 1981 ; 290 (5802 ): 107-113
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  • Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur #MMPMID28769131
  • Hendrickson WA ; Teeter MM
  • Nature 1981[Mar]; 290 (5802 ): 107-113 PMID28769131 show ga
  • 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 ?-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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