Showing papers in "Acta Crystallographica in 1977"

The Structure of Sickling Deer Type III Hemoglobin by Molecular Replacement

Abstract: A combination of oriented single-crystal electron microscopy and protein crystallography has been used to show that crystalline sickling deer hemoglobin molecules from Odocoileus virginianus [oxy fl-chain varianttype III, Hb(DIII)] pack to form a distorted honeycomb (hexagonal) structure with open solvent channels. This network of molecules, consisting of out-of-register anti-parallel strands (fibrils), bears an unmistakable relation to the hemoglobin fibers and aggregates found in human sickled cells. The crystal structure was solved by means of the rotation and translation functions, with data to 3-5/k resolution giving the current residual of 0.430. Oxyor cyanomet-Hb(DIII) crystallizes in space group C2 with a = 163.49 (3), b = 70.83 (2), c= 65.95 (2) A, fl = 94.15 (1) ° and Z = 4.