title: Analysis of the crystal arrangement in collagen fibrils of mineralizing turkey tibia tendon.
abstract: Mineralized pieces of tendons from the tibio-tarsus of turkeys were (i) shock-frozen, freeze-dried, embedded and cut without staining, or (ii) fixed, embedded and stained after sectioning. Micrographs were taken with an electron microscope on longitudinally cut sections. The center-to-center distances of neighboring apatitic needles within collagen fibrils were measured. For shock-frozen and freeze-dried specimens, the average of these distances is 4.7 nm and the most frequent value 4.2 nm; for the fixed and stained specimens, 3.8 nm and 3.6 nm, respectively. Laser diffraction of the electron micrographs showed a dumbbell-like intensity pattern (two diffuse maxima of intensity on the equator, one on each side of the central spot), giving an average distance of about 6 nm. This value represents the upper range of the direct measurements. The measurements demonstrate that the arrangement of the collagen microfibrils is mainly preserved during mineralization. However, using laser diffraction, distances of 9-11 nm were also observed. Such large distances can also be demonstrated by X-ray diffraction on collagen fibrils stained under special conditons. this may indicate that special conditions of apatitic mineralization or staining may alter the arrangement of the microfibrils.
mesh_terms: D000818:Animals; D001031:Apatites / Q000032:analysis; D002113:Calcification, Physiologic; D003094:Collagen / Q000032:analysis*; D003460:Crystallization; D005121:Extremities; D007834:Lasers; D055095:Optics and Photonics; D013710:Tendons / Q000032:analysis / Q000648:ultrastructure*; D014422:Turkeys / Q000033:anatomy & histology*
chemical_list: D001031:Apatites; D003094:Collagen