Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 A resolution.

@article{Wright1987RefinementOT,
  title={Refinement of the crystal structure of wheat germ agglutinin isolectin 2 at 1.8 A resolution.},
  author={Christine Schubert Wright},
  journal={Journal of molecular biology},
  year={1987},
  volume={194 3},
  pages={501-29}
}
The crystal structure of wheat germ agglutinin isolectin 2 has been refined by the restrained least-squares method of Hendrickson & Konnert (1980). The asymmetric unit of the C2 crystals contains two chemically identical promoters related by a non-crystallographic 2-fold screw operation. A total of 2290 protein atoms and 186 ordered water sites refined to a final R-factor of 0.179 and an average B-value of 21.6 A2, using 54% (15,601) of the total possible number of reflections in the resolution… CONTINUE READING

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