Figures and Tables
From the following article:
Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin
Glen Spraggon, Stephen J. Everse and Russell F. Doolittle
Nature 389, 455-462(2 October 1997)
doi:10.1038/38947
Figure 1
Schematic representation of the three polypeptide chains that compose human fibrinogen fragment D.
Full size figure and legend (3K)
Figure 2
a, Ribbon representation of fragment D, showing the region of coiled coils and the globular 
and 
domains.
Figure 3
a, Ribbon representation of fragment D, showing the region of coiled coils and the globular and domains.
Figure 4
a, Topology of -chain (green) and -chain (red) C-terminal domains.
Figure 5
a, Topology of -chain (green) and -chain (red) C-terminal domains.
Figure 6
a, Topology of -chain (green) and -chain (red) C-terminal domains.
Figure 7
Multiple alignment of carboxyl domains of fibrinogen (FBE)- and (FGA)-chains from various species (H, human; F, frog; C, chicken; L, lamprey).
Figure 8
a, Electron-density omit map showing peptide ligand Gly-Pro-Arg-Pro-amide bound to -chain binding site in double-D as calculated with |Fo| - |Fc| coefficients and phases from the refined model contoured at 2.2
.
Figure 9
a, Electron-density omit map showing peptide ligand Gly-Pro-Arg-Pro-amide bound to -chain binding site in double-D as calculated with |Fo| - |Fc| coefficients and phases from the refined model contoured at 2.2.
Figure 10
Four views across the D–D interface as seen from increasing distance.
Full size figure and legend (100K)
Figure 11
Four views across the D–D interface as seen from increasing distance.
Full size figure and legend (46K)
Figure 12
Four views across the D–D interface as seen from increasing distance.
Full size figure and legend (37K)
Figure 13
Four views across the D–D interface as seen from increasing distance.
Full size figure and legend (49K)