An electron microscopic analysis has been made of the various polymorphic forms of fibrous long spacing (FLS) calf-skin collagen, obtained by precipitation in the presence of chondroitin sulphate.Anti-parallel packing of tropocollagen macroniolecules with opposing ends in register is a feature common to all the FLS polymorphic forms. The glycosaminoglycans-mediated intermolecular contacts which lead to this anti-parallel association can also give rise to non-fibrous symmetrical segments. To account for the observed fibrous structures it is sufficient to suppose that two additional glycosaminoglycans-mediated inrermolecular contacts may occur. One of these causes adjoining tropocollagen units to be mutually overlapped by 0.154 L and the other by 0.425 L (L is the length of a tropocollagen macromolecule). These additional contacts may occur separately, giving FLS I and FLS IV respectively, or they may occur together, given FLS II and 111 and more complex structures.In FLS formation, the usual native-type co...