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Structure of human hemoglobin C: a disease with intraerythrocytic crystals

T E Houston, R L Girling, E L Amma

    Biochimica Et Biophysica Acta
    |February 26, 1979
    PubMed

    Insights

    Human cyanomethemoglobin C crystals exhibit dense molecular packing, potentially explaining their facile intraerythrocytic crystallization. This structural insight aids understanding of hemoglobin variants.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Crystallography

    Background:

    • Hemoglobin C is a human hemoglobin variant.
    • Intraerythrocytic crystallization of hemoglobin is a known phenomenon, particularly in certain disease states.
    • Understanding the structural basis of hemoglobin crystallization can provide insights into hemoglobinopathies.

    Purpose of the Study:

    • To determine the crystal structure of human cyanomethemoglobin C.
    • To investigate the packing arrangement of hemoglobin C molecules in crystals.
    • To correlate structural findings with the observed ease of intraerythrocytic crystallization.

    Main Methods:

    • Crystallization of human cyanomethemoglobin C.
    • X-ray diffraction analysis to determine crystal structure and space group (orthorhombic P212121).
    • Single crystal electron microscopy to visualize molecular arrangement.

    Main Results:

    • Human cyanomethemoglobin C crystallized in the orthorhombic space group P212121.
    • Electron micrographs revealed filaments aligned with the b-axis.
    • The crystal structure demonstrated unusually dense packing of hemoglobin molecules compared to other known hemoglobin crystals.

    Conclusions:

    • The dense packing observed in cyanomethemoglobin C crystals may be responsible for its propensity for intraerythrocytic crystallization.
    • Structural data provides a basis for understanding the physical properties of hemoglobin C.
    • Further studies may explore the implications for hemoglobin disorders.

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