The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis).

@article{Ko1993TheTS,
  title={The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis).},
  author={Tzu Ping Ko and Joseph D. Ng and A. Mcpherson},
  journal={Plant physiology},
  year={1993},
  volume={101 3},
  pages={729-44}
}
The three-dimensional structure of the vicilin storage protein canavalin, from Canavalia ensiformis, has been determined in a hexagonal crystal by x-ray diffraction methods. The model has been refined at 2.6 A resolution to an R factor of 0.197 with acceptable geometry. Because of proteolysis, 58 of 419 amino acids of the canavalin polypeptide are not visible in the electron density map. The canavalin subunit is composed of two extremely similar structural domains that reflect the tandem… CONTINUE READING