Precise descriptions of the three-dimensional arrangements of collagen in bone are essential to understand the mechanical properties of this complex tissue. Transmission electron microscopy (TEM) analysis of decalcified human compact bone in section reveals characteristic patterns forming regular series of nested arcs. Such patterns are a direct consequence of an organization described as a twisted plywood and relate the distribution of collagen fibrils in osteons with that of molecules in cholesteric liquid crystals. The hypothesis that liquid crystalline properties are involved in the morphogenesis of dense collagen matrices was supported by data obtained in vitro. At a molecular level, acid-soluble collagen molecules spontaneously assemble, at concentrations of 50mg/ml or more, in precholesteric-banded patterns and cholesteric phases, identified by polarized light microscopy. In a more physiological context, these results were conforted, with the precursor molecule of collagen, procollagen, soluble at neutral pH. This protein spontaneously forms liquid crystalline precholesteric phases corresponding to banded patterns and birefringent cords. Stabilization of the liquid crystalline collagen, induced by pH modification and fibril formation, shows characteristic morphologies in TEM, which directly mimic arrays described in vivo. Undulating fibrils are indeed similar to crimp morphologies described in tendons and continuously twisting fibrils, and give rise to arced patterns similar to supra-molecular architectures identified in compact bone.