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Platelet factor 4. Crystallization and x-ray diffraction studies

K Kurachi

    The Journal of Biological Chemistry
    |November 25, 1978
    PubMed
    Summary
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    Researchers crystallized human platelet factor 4 using ammonium sulfate. Structural analysis revealed orthorhombic crystals with specific unit cell dimensions, suggesting multiple protein molecules per asymmetric unit.

    Area of Science:

    • Protein crystallography
    • Structural biology
    • Biochemistry

    Background:

    • Human platelet factor 4 (PF4) is a chemokine involved in various biological processes.
    • Understanding the three-dimensional structure of PF4 is crucial for elucidating its function.

    Purpose of the Study:

    • To determine the crystal structure of human platelet factor 4.
    • To characterize the unit cell parameters and molecular arrangement within the crystal.

    Main Methods:

    • Crystallization of human platelet factor 4 using ammonium sulfate.
    • X-ray diffraction analysis to determine crystal structure.
    • Unit cell dimension determination (a = 78.7 A, b = 80.6 A, c = 54.6 A).

    Main Results:

    Related Experiment Videos

    • Orthorhombic crystals of human platelet factor 4 were obtained.
    • The space group was identified as P21212.
    • Unit cell volume and protein mass (7800 daltons) indicated the presence of four or five molecules in each asymmetric unit cell.

    Conclusions:

    • The study successfully determined the crystal structure of human platelet factor 4.
    • The structural data provides insights into the quaternary arrangement of PF4 molecules in the crystal lattice.
    • This structural information can aid in understanding PF4's biological interactions and functions.