X-ray scattering studies of glycinin solutions have been extended to higher scattering angles of 2 θ ∼ 0.15 rad. Reproducible, high quality data in the angular range 0.38–6.29 nm −1 have been obtained. Scattering curves show features hitherto unreported that reveal details not only of overall shape and size of the protein but also its internal structure. Analysis suggests that currently accepted models for this protein based on the assumptions of equal-sized, touching spheres are inadequate to describe experimental observations.