Synchrotron SAXS data from solutions of TIP60 (Truncated Icosahedral Protein composed of 60-mer fusion proteins) in 25 mM HEPES, 100 mM NaCl, 1 mM EDTA, 5% glycerol, pH 8 were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK, Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 5 mg/ml were measured at 20°C. 30 successive 5 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
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