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. 2011 Nov 17;7(11):e1002380. doi: 10.1371/journal.ppat.1002380

Figure 3. Structure determination of the CT-Ler/LeeH complex based on NMR and SAXS.

Figure 3

(A) SAXS intensity in logarithmic scale measured for a CT-Ler/LeeH equimolar sample (open circles) as a function of the momentum transfer Inline graphic, where Inline graphic Å is the X-ray wavelength and Inline graphic is the scattering angle. CRYSOL fit of the SAXS curve using a representative NMR structure (red); the average deviation Inline graphic is 1.16. Only the range 0.018< s <0.4 Å−1 is displayed. The point by point deviations [(I(s)exp−I(s)fit)/Inline graphic], where Inline graphic is the experimental error are shown in the bottom panel. (B) Scatter plot of NMR intermolecular restraint violations versus Inline graphic values for the initial set of 400 complex structures and the final ensemble of 20 low energy structures highlighted in red (inset). The main panel shows a zoom of the best structures. (C) Backbone overlap of the 20 lowest energy complex structures. Protein backbone is coloured in rainbow gradation.