Crystal structure of native chicken fibrinogen at 5.5-angstrom resolution

The crystal structure of native chicken fibrinogen has been determined at a resolution of 5.5 Angstrom. The full-length molecule is 460 Angstrom in le ngth and sigmoidally shaped. The structure includes the full sweep of the c oiled 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 outl ines of disordered alpha C domains nestled within the confines of the sinuo us coiled coils. The amino-terminal segments of the alpha- and beta-chains, including the fibrinopeptides A and B, are also disordered.