Sokolova et al. 10.1073/pnas.0603629103.

Supporting Information

Files in this Data Supplement:

Supporting Text
Supporting Figure 5
Supporting Figure 6
Supporting Movie 1
Supporting Movie 2
Supporting Movie 3
Supporting Figure 7




Supporting Figure 5

Fig. 5. Concentration dependence of vimentin assembly. (A) Scattering from the K139C mutant in 20 mM NaCl and 5 mM Tris·HCl (pH 8.4) at 2.5, 6.5, and 18 mg/ml protein (blue circles, red squares, and green triangles, respectively). (B) Corresponding pcr(r) functions.





Supporting Figure 6

Fig. 6. Refinement of tetramer and octamer models. (A) Goodness-of-fit between the calculated scattering from the tetramer model and the experimental data as a function of the distance dtetra between the dimers' axes. (B) 2D plot showing the goodness-of-fit between the calculated and experimental scattering curves as a function of the separation between the adjacent dimers docta and the angle a (see Fig. 3D for definitions).





Supporting Figure 7

Fig. 7. Example of SAXS data interpretation for polydisperse samples. Shown are experimental scattering curves for solutions of vimentin K139C mutant in 20 mM NaCl and 5 mM Tris·HCl (pH 8.4) at 2.5, 6.5, and 18 mg/ml (blue, green. and red dots, respectively) together with calculated scattering for the corresponding mixtures of oligomers (see Table 1). The two latter curves were vertically displaced for visibility.





Supporting Movie 1

Movie 1. Final vimentin tetramer model.





Supporting Movie 2

Movie 2. Final vimentin octamer model.





Supporting Movie 3

Movie 3. Final vimentin unit-length filament model.