Refined structure of dimeric diphtheria toxin at 2.0 A resolution.

@article{Bennett1994RefinedSO,
  title={Refined structure of dimeric diphtheria toxin at 2.0 A resolution.},
  author={Melanie J. Bennett and Sun Hui Choe and David S Eisenberg},
  journal={Protein science : a publication of the Protein Society},
  year={1994},
  volume={3 9},
  pages={1444-63}
}
The refined structure of dimeric diphtheria toxin (DT) at 2.0 A resolution, based on 37,727 unique reflections (F > 1 sigma (F)), yields a final R factor of 19.5% with a model obeying standard geometry. The refined model consists of 523 amino acid residues, 1 molecule of the bound dinucleotide inhibitor adenylyl 3'-5' uridine 3' monophosphate (ApUp), and 405 well-ordered water molecules. The 2.0-A refined model reveals that the binding motif for ApUp includes residues in the catalytic and… CONTINUE READING

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