Bayesian refinement of protein structures and ensembles against SAXS data using molecular dynamics
Fig 5
Residuals between the calculated SAXS curves and the experimental SAXS curves, evaluated at the q-points applied during the refinement simulations of Hsp90 (color code see legend).
(A) Residuals ΔI/σexp normalized with respect to purely statistical experimental errors σexp. Large residuals at low q reflect that the MD force field prohibited structures that would accurately match the data within statistical errors. (B) Residuals ΔI(q)/σtot, where σtot denotes the total error including both statistical and estimated systematic errors (see Methods for details). The reduced residuals compared to panel (A) reflect that the Bayesian analysis suggested substantial systematic errors as the most plausible explanation for discrepancies between calculated and experimental SAXS curves.