Biochemical and X-Ray Diffraction Analysis of Concanavalin B Crystals from Jack Bean

Parallel biochemical and crystallographic studies have been carried out on the protein concanavalin B from Jack Bean (Canavalis ensiformis). The studies show the protein to be a monomer of 33,000 daltons with unexceptional amino acid composition and no covalently bound carbohydrate. The molecule contains a single, firmly bound zinc ion and we present evidence that the protein specifically binds nucleotide coenzymes including at least NADPH and...