SEC-SAXS analysis of NLRP1(227–990).

Abstract

(A) Scattering data obtained on two protein samples with concentrations of 2 mg/mL (open circles) and 6 mg/mL (open squares) respectively. (B) The linear low-q regions of the scattering curves used for the Guinier analysis. (C) Kratky analysis performed on the data sets at two different concentrations. (D) Normalized inter-atomic pairwise distribution function, P(r), calculated for the two concentrations used in the analysis, showing a maximum particle size of about 115 Å. (E and F) Fitting of the experimental SAXS curve at 2 mg/mL (open circle) with the structure of NLRC4 in two different conformations, open conformation (derived from PDB 3jbl) and closed conformation (derived from PDB 4kxf); the residual difference between the experimental and the calculated values of Log[I(q)] are reported for both fits. In both cases the fitting structures were truncated to residues 93–793 which represent the region that is homologous to the NLRP1 construct used for the SAXS analysis.</p