Synchrotron SAXS data from solutions of Herpes simplex virus 1 tegument protein UL11 in 50 mM HEPES, 100 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS, Ithaca, NY, USA) using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.124612 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size exclusion chromatography SAXS (SEC-SAXS) was performed at 25°C using a sample injection concentration of 18.00 mg/ml. 497 successive 2 second data frames were collected through the SEC elution profile. Data corresponding to the UL11 elution peak were normalized to the intensity of the transmitted beam and radially averaged. Normalized and reduced SAXS data corresponding to solvent-blank ('solute-free' buffer) from the SEC column were subtracted.