Small-angle X-ray scattering studies of the linear PvRON2 (2035–2074) peptide and PvAMA1-His6. SAXS data from solution containing the recombinant PvAMA1-His6 protein and linear PvRON2 (2035–2074) peptide. The results show the formation of aggregates under the experimental conditions used in the study. a The red line corresponds to the best model fitting the data (χ2 = 2.57). Insets: P(r) function obtained through indirect Fourier transform shows the presence of aggregates with maximum sizes close to 370 Å. b The average 3D model reconstructed from the P(r) function indicates aggregates with irregular shape. The aggregates in solution have dimensions about four times bigger than the complex between PvAMA1-PvRON2sp1 previously reported by Vulliez-Le Normand et al.