X-ray diffraction studies of fibrillin-rich microfibrils: Effects of tissue extension on axial and lateral packing

T. J. Wess, P. P. Purslow, C. M. Kielty

    Research output: Contribution to journalArticlepeer-review

    Abstract

    X-ray diffraction of hydrated fibrillin rich microfibrils, in the form of zonular filaments from bovine eyes, demonstrated meridional diffraction peaks indexing on a fundamental periodicity of ~56 nm in the relaxed state. The effect of sample extensions of up to 50% in length produced an increase in the axial periodicity of only 4% as judged by alteration of the diffraction peak position of the third meridional order. This effect was shown to be reversible. Further extension to 100% of the tissue rest length caused extensive deterioration in the quality of the diffraction and resulted in a more complex meridional diffraction series, where the fundamental axial periodicity also changed to a length of approximately 80 nm. The fibrillin diffraction image also contains an equatorial diffraction peak that is enhanced upon tissue extension. The measurement of the molecular spacing from the equatorial diffraction profile indicated that the closest approach of molecules gave a broad interference peak of spacing 28 nm, this is nearly twice the molecular diameter as estimated from electron microscopy of dehydrated samples.
    Original languageEnglish
    Pages (from-to)123-127
    Number of pages4
    JournalJournal of Structural Biology
    Volume122
    Issue number1-2
    DOIs
    Publication statusPublished - 1998

    Keywords

    • Fibrillin-rich microfibrils
    • Structure
    • X-ray diffraction

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