The calculated p functions for the monomer and dimer have their maxima in the same positions as the maxima of the functions calculated using raw experimental data at various salt concentrations, confirming that the MCR-ALS analysis is accurate. The first insights into the full-length structure of the barley SGT1 protein were performed using the ab initio shape determination method. The pure scattering function for the monomeric SGT1 protein, taken from the MCR-ALS analysis, was used to obtain the low-resolution structure in solution using the ab-initio approach implemented in the Oleanolic DAMMIN program. The packing radius of the dummy atoms was 0.6 nm, and the total number of non-solvent dummy atoms was approximately 5300. During the modeling process, symmetry and shape restrains were not imposed. The final model obtained after averaging 10 independent DAMMIN models is presented in Figure 9. The monomeric form of the barley SGT1 protein has an elongated shape, with a bend in the middle of the molecule. All three structures of barley SGT1 domains can be unambiguously fit into the DAMMIN model. To fit the SGT1 domains into the low-resolution model of the full length SGT1 protein, the regions between these domains must be elongated and must therefore be unfolded or have very little secondary structure content. The Folinic acid calcium salt pentahydrate sequences of the VR1 and VR2 regions are much shorter in the barley SGT1 than in the folded domains, but in our model these regions have nearly the same dimensions as the folded domains. To independently confirm these assumptions, another low-resolution modeling program, GASBOR, was used. The GASBOR model had a very similar geometry, with an elongated shape and a slight bend in the region in which the CS domain is located. The low resolution models from DAMMIN and GASBOR fit very well to the experimental monomeric barley SGT1 scattering curve, as presented in Figure 9. The same methodology was also applied to obtain the low-resolution shape of the barley SGT1 dimer.The low-resolution molecular model of the dimer obtained from DAMMIN has an elongated shape, similar to that observed for the SGT1 monomer.