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Polyoma virion and capsid crystal structures.

K W Adolph, D L Caspar, C J Hollingshead

    Science (New York, N.Y.)
    |March 16, 1979
    PubMed
    Summary
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    X-ray diffraction reveals virus particles and empty capsids crystallize identically. Electron microscopy shows the protein coat

    Area of Science:

    • Structural biology
    • Virology
    • Biophysics

    Background:

    • Viruses are complex biological entities with intricate structures.
    • Understanding viral structure is crucial for developing antiviral strategies.
    • Previous studies have provided insights into viral morphology.

    Purpose of the Study:

    • To elucidate the crystallographic and structural characteristics of complete virus particles and empty capsids.
    • To determine the influence of the protein coat's surface morphology on X-ray diffraction patterns.
    • To enable detailed analysis of the viral chromatin core's structure and variability.

    Main Methods:

    • X-ray diffraction was employed to analyze the crystallization of virus particles and capsids.
    • Electron microscopy was used to visualize the surface morphology of the viral protein coat.

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  • Comparison of electron density maps was utilized for structural analysis.

    • Main Results:

    • Complete virus particles and empty capsids exhibit isomorphic crystallization.
    • The protein coat's surface morphology significantly influences X-ray reflection intensities up to 30 angstroms resolution.
    • Electron density maps allow for the analysis of the viral chromatin core's structure.

    Conclusions:

    • The study provides a detailed structural understanding of virus particles and capsids.
    • The findings highlight the critical role of the protein coat in determining diffraction patterns.
    • This work facilitates further investigation into the viral chromatin core.