The majority of collagen in the extracellular matrix is found in a fibrillar form, with long slender filaments each displaying a characteristic approximately 67?nm D-repeat. Here they provide the stiff resilient part of many tissues, where the inherent strength of the collagen triple helix is translated through a number of hierarchical levels to endow that tissue with its specific mechanical properties. A number of collagen types have important structural roles, either comprising the core of the fibril or decorating the fibril surface to give enhanced functionality. The architecture of subfibrillar and suprafibrillar structures (such as microfibrils), lateral crystalline and liquid crystal ordering, interfibrillar interactions, and fibril bundles is described. The fibril surface is recognized as an area that contains a number of intimate interactions between different collagen types and other molecular species, especially the proteoglycans. The interplay between molecular forms at the fibril surface is discussed in terms of their contribution to the regulation of fibril diameter and their role in interfibrillar interactions.