Abstract
Three-dimensional reconstruction of electron micrographs of the 20-nm diameter fibres of HbS reveals an inner helical core of four strands surrounded by an outer helix of 10 strands to give a total of 14 strands. The strands are arranged with roughly hexagonal packing to produce an unusual helical structure which features a variety of intermolecular contacts and a non-circular cross section.
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Dykes, G., Crepeau, R. & Edelstein, S. Three-dimensional reconstruction of the fibres of sickle cell haemoglobin. Nature 272, 506–510 (1978). https://doi.org/10.1038/272506a0
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DOI: https://doi.org/10.1038/272506a0
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