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Three-dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 3.5 Å Resolution

An Erratum to this article was published on 14 November 1970

Abstract

Electron density maps of human deoxyhaemoglobin at a resolution of 3.5 Å reveal new conformations of the C-terminal residues of the β chain and confirm their contribution to the alkaline Bohr effect. A preliminary comparison of this structure with that of horse oxyhaemoglobin shows that the main differences occur at the chain termini and at certain side chains in the α1β2 interface.

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MUIRHEAD, H., GREER, J. Three-dimensional Fourier Synthesis of Human Deoxyhaemoglobin at 3.5 Å Resolution. Nature 228, 516–519 (1970). https://doi.org/10.1038/228516a0

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