To assess the impact of the number of elements in a system on the speed of SAS intensity calculation, we compared the time required by the PLUMED to determine intensities from MD trajectory frames. We used different resolutions, including all-atom (AA), Martini scheme with transferable parameters (MT), and single-bead per amino acid (1B) / three-beads per nucleotide (3B) mappings with the corresponding transferable parameters. For the analysis, we selected a GSN trajectory consisting of 6,442 frames to evaluate the performance on proteins, and a 500 frames trajectory of a large subunit ribosome fragment to evaluate nucleic acids. The intensities were calculated for 31 𝑞 values, in the range 1⋅10 -10 Å -1 to 0. In addition to performance evaluation, we also assessed the accuracy of 1B/3B mappings and parameters in the calculation of scattering intensities. For this benchmark, we selected 6,442 equidistant frames from the GSN MD simulation, 6,502 from B1, 9,622 from GFP and 7,256 from the 12-mer RNA strand and calculated the SAXS and SANS intensity in both coarsegrained and atomistic detail for 201 𝑞 values, in the range 1⋅10 -10 Å -1 to 0.5 Å -1 , every 0.0025 Å - 1 . For each frame and each 𝑞 value, the intensity calculated with 1B/3B was compared with the corresponding intensity at atomistic resolution, which was taken as the reference. For SAXS we also included the comparison between MT and AA. The GSN SAXS intensities calculated with 1B mapping better agree with those obtained with AA resolution than with MT up to 0.3 Å -1 , since the difference (residuals) between 1B and AA intensities is smaller than the difference between MT and AA for the same set of 𝑞 values (Figure ). A similar behaviour has been observed also for B1 (Figure , left panel) and GFP (Figure , left panel) SAXS intensities.