Figure 1. Schematic representation of a SAS experiment (k ₀ is the wave vector of the incoming radiation, k ₁ is the wave vector of the scattered beam).

Figure 2. Scattering profiles and overall structural information. (Middle panel) Typical SAXS patterns before and after buffer subtraction. (Left) Guinier plot provides the radius of gyration and molecular weight. (Bottom) Kratky plot allows for an assessment of protein folding. (Top right) Porod plot defines the particle volume. The datasets are presented on relative scale.

Figure 3. Complementarity of SAS and NMR. Solution scattering defines the overall dimensions and shape, and is sensitive to translations, while NMR provides information about local interfaces and orientations.

Figure 4. Models of tumor suppressor p53 generated from the SAXS curves (intensity versus scattering angle: dots, experimental data; solid lines, computed patterns). (a) Full‐length p53 in the free form. The four domains of p53 recognizing DNA (green and cyan) are arranged in two separated dimers. (b) Truncated p53 in complex with DNA. The core domains are wrapped around DNA (pink). The available high‐resolution structures of the domains employed in the modeling are displayed as ribbons, the flexible portions of p53 as semitransparent beads.