Updated consensus SAS profiles generated using the MLSAScombine tool (with logs binning) for ribonuclease A in 50 mM Tris pH 7.5, 100 mM NaCl. A total of 24 independent SAXS profiles (6 SECSAXS and 18 batch SAXS) contributed from 9 SAXS beamlines were combined. The minimum s value for SECSAXS data was 0.05 nm1. Protein concentrations for batch measurements ranged from 0.1  6 mg/mL, and the minimum s value for these data (no less than 0.76 nm1) was chosen to ensure exclusion of lows data points affected by aggregation. The ribonuclease A atomistic model for CRYSOL, PepsiSAXS, and FoXS calculations is the PDB ID 7RSA with smallmolecule crystallisation agents removed. Custom WAXSiS calculations used the same coordinates with added explicit waters and ions to match the experimental conditions for the MD simulations. WAXSiS calculations include statistical errors and the error weighting for residual differences is therefore the square root of the sum of the squares of the experimental and WAXSiS statistical errors. Model fits are shown in order (top to bottom): FoXS, CRYSOL (classic directional hydration layer), PepsiSAXS and custom WAXSiS. All three model fits with implicit hydration layer are to data on a log sscale, while for custom WAXSiS the data are on a linear sscale. The unusually good statistics for the consensus SAXS data generally give rise to large χsquare values for the model fits.
Additional data and information are made available in the fullentry zip archive and include: i) The input data for MLSAScombine; ii) Runscripts used with MLSAScombine; iii) Output files for updated consensus files from MLSAScombine with log and linear sbinning; iv) Output files for combined SECSAS data from MLSAScombine with log sbinning and; v) The original customWAXSiS modelfits with errors with the consensus data on the same sgrid.

