Abstract
The X-ray structure of cyanomet human hemoglobin C has been solved and refined, R ∼27%. The molecular packing can be represented in two dimensions by two sets of parallel strands, one set in the b direction and the other in the c direction. Taken together the two sets of strands interconnect the molecules into square nets or layers where each molecule contacts its four nearest neighbors. Molecules in one layer are displaced in a and b so that they fit into the “holes” of the square arrays of the adjacent layers (normal to a ) resulting in a pseudo body-centered cubic packing. This packing can account for the hemoglobin crystallization in and fragility of the erythrocytes. The aberrant β6A3 Lys residue is in a position to influence the crystal formation.
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