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Interfibrillar packing of bovine cornea by table‐top and synchrotron scanning SAXS microscopy
Author(s) -
Sibillano T.,
De Caro L.,
Scattarella F.,
Scarcelli G.,
Siliqi D.,
Altamura D.,
Liebi M.,
Ladisa M.,
Bunk O.,
Giannini C.
Publication year - 2016
Publication title -
journal of applied crystallography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.429
H-Index - 162
ISSN - 1600-5767
DOI - 10.1107/s1600576716010396
Subject(s) - small angle x ray scattering , synchrotron , synchrotron radiation , materials science , cornea , microscopy , scattering , crystallography , collagen fibril , hexagonal crystal system , optics , chemistry , biophysics , physics , biology
Bovine cornea was studied with scanning small‐angle X‐ray scattering (SAXS) microscopy, by using both synchrotron radiation and a microfocus laboratory source. A combination of statistical (adaptive binning and canonical correlation analysis) and crystallographic (pair distribution function analysis) approaches allowed inspection of the collagen lateral packing of the supramolecular structure. Results reveal (i) a decrease of the interfibrillar distance and of the shell thickness around the fibrils from the periphery to the center of the cornea, (ii) a uniform fibril diameter across the explored area, and (iii) a distorted quasi‐hexagonal arrangement of the collagen fibrils. The results are in agreement with existing literature. The overlap between laboratory and synchrotron‐radiation data opens new perspectives for further studies on collagen‐based/engineered tissues by the SAXS microscopy technique at laboratory‐scale facilities.