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.

journal_name

Phys Med Biol

authors

Suhonen H,Fernández M,Serimaa R,Suortti P

doi

10.1088/0031-9155/50/22/012

subject

Has Abstract

pub_date

2005-11-21 00:00:00

pages

5401-16

issue

22

eissn

0031-9155

issn

1361-6560

pii

S0031-9155(05)95488-2

journal_volume

50

pub_type

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