Extended Data Figure 8: SAXS of PfRH5 in complex with growth-inhibitory Fab fragments.
From: Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodies
a, The theoretical scattering calculated from the average of 20 ab initio reconstructions (continuous lines, with PfRH5 in orange, PfRH5–9AD4 in green, PfRH5–QA1 in red, and PfRH5–QA5 in blue) plotted with the experimental scattering intensity curves (black diamonds). The data are presented as the natural logarithm of the intensity. The Guinier plots are displayed in the inset. b, The distance distribution function, P(r), with colours as in a. c, The crystal structures of PfRH5ΔNL–QA1(left) and PfRH5ΔNL–9AD4 (middle) were docked into the corresponding full-length PfRH5–Fab envelopes (grey). PfRH5ΔNL is shown in yellow, QA1 in red, and 9AD4 in green. PfRH5ΔNL and a Fab fragment (cyan) were docked into the PfRH5–QA5 SAXS envelope to generate a model of the PfRH5–QA5 structure (right). d, A summary of SAXS parameters. The radius of gyration (Rg) was determined from the Guinier plot using AutoRg37, and the maximum particle dimension (Dmax) and the Porod volume39 were calculated using GNOM37. An estimate of the molecular weight was obtained by dividing the Porod volume by 1.7. Ab initio modelling was used to generate 20 shape reconstructions from the data. The normalized spatial discrepancy parameter (NSD) diagnoses the similarity of these models42. The models were averaged and the fit of the average model to the experimental data are indicated by the χ value.
