Abstract
Despentapeptide insulin, prepared by removing the five C-terminal B-chain residues, occurs in several crystal forms. The relationship between these and the known pig 2-Zn insulin structure is analysed by the fast rotation function and R-factor searches. Reasonably good models were obtained even in the cases when there are two molecules in an asymmetric unit. The 2-Zn insulin coordinates were positioned in the C2 sheep cell and refinement commenced using the fast Fourier least-squares method. The packing of this modified insulin is quite different from that of all other insulins studied so far but the molecular structure is similar to that of 2-Zn insulin.
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