Crystal structure of native chicken fibrinogen at 5.5-Å resolution

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Abstract
The crystal structure of native chicken fibrinogen has been determined at a resolution of 5.5 Å. The full-length molecule is 460 Å in length and sigmoidally shaped. The structure includes the full sweep of the coiled coils that connect the central and terminal domains; the chain paths of the central domain confirm a predicted scheme of planar disulfide rings in apposition with each other. Electron density maps have revealed the outlines of disordered αC domains nestled within the confines of the sinuous coiled coils. The amino-terminal segments of the α- and β-chains, including the fibrinopeptides A and B, are also disordered.