The small angle X-ray scattering from unheated and heated calcified chicken tendon has been accurately measured using an automatically recording Kratky camera. A two-dimensional optical diffraction pattern of electron micrographs has been recorded and is in excellent agreement with the small angle X-ray diffraction pattern.
The wide and small angle X-ray diffraction pattern, the Fraunhofer diffraction pattern, electron microscopic appearance, and a Fourier synthesis are mutually consistent, and indicate that the crystalline fraction of apatite in normal calcified tendon exists in the form of well oriented crystallites of about 330 Å in length and 50–60 Å in width with the long axis being parallel to the local fibre axis. The separate crystallites are largely located in parallel rows which repeat every 660 Å in the longitudinal direction of the tendon.
Analysis of the small angle equatorial scattering shows the crystallites to be clustered together into three well-defined groups with diameters of about 60 Å, 190 Å, and 400 Å. It is suggested that the largest clusters are located in between the collagen fibrils and correspond to the primary calcification.
KeywordsFibril Apatite Collagen Fibril Crystalline Fraction Optical Diffraction
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