Crystal and molecular structures of human progastricsin at 1.62 A resolution.

@article{Moore1995CrystalAM,
  title={Crystal and molecular structures of human progastricsin at 1.62 A resolution.},
  author={Sheila A. Moore and Anita R. Sielecki and Maia M. Chernaia and Nadezhda I. Tarasova and Michael N. G. James},
  journal={Journal of molecular biology},
  year={1995},
  volume={247 3},
  pages={
          466-85
        }
}
The crystal and molecular structures of human progastricsin (hPGC) have been determined using multiple isomorphous replacement methods and anomalous scattering in conjunction with a phased translation function. The structure has been refined to a conventional R-factor (= sigma parallel Fo magnitude of - magnitude of Fc parallel / sigma magnitude of Fo magnitude of) of 0.179 with data to 1.62 A resolution. The first 37 amino acid residues of the prosegment are similar in conformation to the… CONTINUE READING
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