HIGH-RESOLUTION STRUCTURES OF SINGLE-METAL-SUBSTITUTED CONCANAVALIN-A- THE CO,CA-PROTEIN AT 1.6-ANGSTROM AND THE NI,CA-PROTEIN AT 2.0-ANGSTROM

The molecular structures of cobalt- and nickel-substituted concanavali n A have been refined at 1.6 and 2.0 angstrom resolution, respectively . Both metal derivatives crystallize in space group I222 with approxim ate cell dimensions a = 89, b = 87 and c = 63 angstrom and one monomer in the asymmetric unit. The final R factor for Co-substituted concana valin A is 17.8% for 29211 reflections with F > 1.0 sigma(F) between 8 .0 and 1.6 angstrom. For Ni-substituted concanavalin A the final R fac tor is 15.9% for 16128 reflections with F > 1.0sigma(F) between 8.0 an d 2.0 angstrom resolution. Both structures contain a transition-metal binding site and a calcium-binding site but, unlike Cd-substituted con canavalin A, do not have a third metal-binding site. The Co-substitute d concanavalin A structure diffracts to the highest resolution of any concanavalin A structure reported to date. A comparison of the structu res of Ni-, Co-, Cd-substituted and native concanavalin A gives an ind ication of coordinate errors, which is a useful baseline for compariso ns with saccharide complexes of concanavalin A described in other work . We also give a detailed account of multiple conformations which were found for five side-chain residues.