Figure 2.
Cryo-EM structure of FVIII/VWF-DʹD3 complex solved to 2.9 Å resolution. (A) Single micrograph of BIVV001 particles at ×81 000 magnification. Black arrows indicate BIVV001 particles. (B) Representative 2-dimensional class averages of BIVV001, demonstrating multiple particle orientations. Side views were readily observed (middle top and middle bottom) and were the preferred orientation; front-on views (left top and left bottom) and top/other views (right) were also found. (C) Local resolution gradient across EM potential map, colored from high (blue, 2.75 Å) to low (red, 4.75 Å). The core of FVIII is the best resolved portion of the structure, with VWF-D3 the least well resolved. (D) EM potential map colored according to protein domain identity. (E) Representation of FVIII/VWF-D′D3 complex structure. Bound metal ions are depicted as spheres.

Cryo-EM structure of FVIII/VWF-DʹD3 complex solved to 2.9 Å resolution. (A) Single micrograph of BIVV001 particles at ×81 000 magnification. Black arrows indicate BIVV001 particles. (B) Representative 2-dimensional class averages of BIVV001, demonstrating multiple particle orientations. Side views were readily observed (middle top and middle bottom) and were the preferred orientation; front-on views (left top and left bottom) and top/other views (right) were also found. (C) Local resolution gradient across EM potential map, colored from high (blue, 2.75 Å) to low (red, 4.75 Å). The core of FVIII is the best resolved portion of the structure, with VWF-D3 the least well resolved. (D) EM potential map colored according to protein domain identity. (E) Representation of FVIII/VWF-D′D3 complex structure. Bound metal ions are depicted as spheres.

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