Fig. 3.
Fig. 3. Fitting of the FVIII domains within the 3D electron density map. / The alpha-carbon (Cα) chains of the 5 FVIII domains are presented as worms: A1 domain residues colored in red, A2 in yellow, A3 in green, C1 in magenta, and C2 in cyan. Domains were fitted within the 3D density corresponding to one membrane-bound molecule contoured at 0.4ς. Panel A indicates the top view, toward the membrane surface. The 5 protein domains fit well within the electron density. The matching minimum protein density areas are marked with black spheres. Panels B and C show views along the y- and x-axes, respectively, parallel to the membrane surface (black dashed line marked M). The Cα chains are fitted to the 3D density of one molecule following the strongest density distribution, as the contour at 0.4ς could not accommodate all loops of the protein model.

Fitting of the FVIII domains within the 3D electron density map.

The alpha-carbon (Cα) chains of the 5 FVIII domains are presented as worms: A1 domain residues colored in red, A2 in yellow, A3 in green, C1 in magenta, and C2 in cyan. Domains were fitted within the 3D density corresponding to one membrane-bound molecule contoured at 0.4ς. Panel A indicates the top view, toward the membrane surface. The 5 protein domains fit well within the electron density. The matching minimum protein density areas are marked with black spheres. Panels B and C show views along the y- and x-axes, respectively, parallel to the membrane surface (black dashed line marked M). The Cα chains are fitted to the 3D density of one molecule following the strongest density distribution, as the contour at 0.4ς could not accommodate all loops of the protein model.

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