Beschreibung:
<jats:p>The conformation of the Fab and Fc fragments from the human immunoglobulin molecule Kol [IgG I, χ<jats:sub>2</jats:sub>γ<jats:sub>2</jats:sub>, Gm(f)<jats:sup>+</jats:sup>] was studied by small‐angle X‐ray scattering in solution. The fragments were studied in 0.02 M Tris‐HCI buffer. For the Fab fragment the radius of gyration was found to be 3.15 ± 0.15 nm, the volume to be 75 ± 8 nm<jats:sup>3</jats:sup>. For the Fc fragment the respective values were 3.15 ± 0.15 nm for the radius of gyration and 91 ± 8 nm<jats:sup>3</jats:sup> for the volume. A large number of models were calculated for both fragments to find models which fit these data and have the same scattering curve. The models with the best agreement were compared with the models found for the crystalline state by crystal X‐ray studies.</jats:p>