Simulation of small-angle x-ray scattering from collagen fibrils and comparison with experimental patterns

Heikki Suhonen, Manuel Fernandez, Ritva Serimaa, Pekka Suortti

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    Kuvaus

    Simulation of small-angle x-ray scattering from collagen in healthy and cancerous breast tissue may reveal detailed information on the structural changes in collagen. Collagen fibril is modelled as a cylinder with axially periodic step-function electron density, and packing is approximated by placing the cylinders in small hexagonal bundles. The intensity from a bundle is calculated by summing analytical scattering amplitudes from the cylinders, and intensities from several bundles with varying lattice constants are averaged. Comparisons with more complex models are made to estimate the robustness of the model. The oscillations in the equatorial direction are not significantly affected by added complexity. The relative intensities of the Bragg peaks in the meridional direction can be tuned by modifying the axial electron density distribution. Tests with different fibril radius distributions show that the average radius can be determined with an accuracy of +/- 0.5 nm but that the shape of the radius distribution cannot be accurately determined from the scattering patterns. The effect of multiple scattering and the detector point-spread function (PSF) is considered, and the PSF may make a significant contribution to the final slope of the scattering pattern. Comparisons with observed scattering indicate that the model is basically correct at the supra-molecular level.
    Alkuperäiskielienglanti
    LehtiPhysics in Medicine and Biology
    Vuosikerta50
    Numero22
    Sivut5401-5416
    Sivumäärä16
    ISSN0031-9155
    DOI - pysyväislinkit
    TilaJulkaistu - 2005
    OKM-julkaisutyyppiA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä, vertaisarvioitu

    Lainaa tätä

    @article{7859eb217823478888b4bdbdaec504cd,
    title = "Simulation of small-angle x-ray scattering from collagen fibrils and comparison with experimental patterns",
    abstract = "Simulation of small-angle x-ray scattering from collagen in healthy and cancerous breast tissue may reveal detailed information on the structural changes in collagen. Collagen fibril is modelled as a cylinder with axially periodic step-function electron density, and packing is approximated by placing the cylinders in small hexagonal bundles. The intensity from a bundle is calculated by summing analytical scattering amplitudes from the cylinders, and intensities from several bundles with varying lattice constants are averaged. Comparisons with more complex models are made to estimate the robustness of the model. The oscillations in the equatorial direction are not significantly affected by added complexity. The relative intensities of the Bragg peaks in the meridional direction can be tuned by modifying the axial electron density distribution. Tests with different fibril radius distributions show that the average radius can be determined with an accuracy of +/- 0.5 nm but that the shape of the radius distribution cannot be accurately determined from the scattering patterns. The effect of multiple scattering and the detector point-spread function (PSF) is considered, and the PSF may make a significant contribution to the final slope of the scattering pattern. Comparisons with observed scattering indicate that the model is basically correct at the supra-molecular level.",
    author = "Heikki Suhonen and Manuel Fernandez and Ritva Serimaa and Pekka Suortti",
    year = "2005",
    doi = "10.1088/0031-9155/50/22/012",
    language = "English",
    volume = "50",
    pages = "5401--5416",
    journal = "Physics in Medicine and Biology",
    issn = "0031-9155",
    publisher = "IOP Publishing",
    number = "22",

    }

    Simulation of small-angle x-ray scattering from collagen fibrils and comparison with experimental patterns. / Suhonen, Heikki; Fernandez, Manuel; Serimaa, Ritva; Suortti, Pekka.

    julkaisussa: Physics in Medicine and Biology, Vuosikerta 50, Nro 22, 2005, s. 5401-5416.

    Tutkimustuotos: ArtikkelijulkaisuArtikkeliTieteellinenvertaisarvioitu

    TY - JOUR

    T1 - Simulation of small-angle x-ray scattering from collagen fibrils and comparison with experimental patterns

    AU - Suhonen, Heikki

    AU - Fernandez, Manuel

    AU - Serimaa, Ritva

    AU - Suortti, Pekka

    PY - 2005

    Y1 - 2005

    N2 - Simulation of small-angle x-ray scattering from collagen in healthy and cancerous breast tissue may reveal detailed information on the structural changes in collagen. Collagen fibril is modelled as a cylinder with axially periodic step-function electron density, and packing is approximated by placing the cylinders in small hexagonal bundles. The intensity from a bundle is calculated by summing analytical scattering amplitudes from the cylinders, and intensities from several bundles with varying lattice constants are averaged. Comparisons with more complex models are made to estimate the robustness of the model. The oscillations in the equatorial direction are not significantly affected by added complexity. The relative intensities of the Bragg peaks in the meridional direction can be tuned by modifying the axial electron density distribution. Tests with different fibril radius distributions show that the average radius can be determined with an accuracy of +/- 0.5 nm but that the shape of the radius distribution cannot be accurately determined from the scattering patterns. The effect of multiple scattering and the detector point-spread function (PSF) is considered, and the PSF may make a significant contribution to the final slope of the scattering pattern. Comparisons with observed scattering indicate that the model is basically correct at the supra-molecular level.

    AB - Simulation of small-angle x-ray scattering from collagen in healthy and cancerous breast tissue may reveal detailed information on the structural changes in collagen. Collagen fibril is modelled as a cylinder with axially periodic step-function electron density, and packing is approximated by placing the cylinders in small hexagonal bundles. The intensity from a bundle is calculated by summing analytical scattering amplitudes from the cylinders, and intensities from several bundles with varying lattice constants are averaged. Comparisons with more complex models are made to estimate the robustness of the model. The oscillations in the equatorial direction are not significantly affected by added complexity. The relative intensities of the Bragg peaks in the meridional direction can be tuned by modifying the axial electron density distribution. Tests with different fibril radius distributions show that the average radius can be determined with an accuracy of +/- 0.5 nm but that the shape of the radius distribution cannot be accurately determined from the scattering patterns. The effect of multiple scattering and the detector point-spread function (PSF) is considered, and the PSF may make a significant contribution to the final slope of the scattering pattern. Comparisons with observed scattering indicate that the model is basically correct at the supra-molecular level.

    U2 - 10.1088/0031-9155/50/22/012

    DO - 10.1088/0031-9155/50/22/012

    M3 - Article

    VL - 50

    SP - 5401

    EP - 5416

    JO - Physics in Medicine and Biology

    JF - Physics in Medicine and Biology

    SN - 0031-9155

    IS - 22

    ER -