Abstract

We have developed a modeling system for generating density distributions of deoxyhemoglobin S (HbS) polymers that is based on the crystallographic atomic coordinates of HbS. Computed density projections depicting the particle structure may be compared to electron micrographs of negativelystained preparations of sickle hemoglobin. In this manner, image features may be quantitatively analyzed and related to the molecular arrangement of hemoglobin tetramers. Such computer-simulated models provide a structural approach that is able to link high-resolution x-ray diffraction data to electron microscopic studies of noncrystalline polymers of HbS.

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