Fig. 2

GASBOR/DAMMIN-Fit and “solution structure” images of the individual enzymes. a Cel48S-t; left panel: comparison between the experimental SAXS data (red points) and the scattering intensity I(q) of the Cel48S-t envelope obtained by GASBOR (black line) [72], and with that of the constructed structural model using CRYSOL (light blue line) [40]; residuals are illustrated for the envelope calculation; right panel (top): SAXS-derived structural model of the full-length cellulase Cel48S-t. The catalytic domain is separated from the dockerin domain by a linker in an extended conformation; right panel (bottom): comparison between the SAXS-derived structural model (blue) and the molecular envelope generated using GASBOR (transparent grey) [73]. b Cel9A-r; left panel: experimental curve fitted by DAMMIN (black line) [44] and CRYSOL (light blue line) [40] using the coarse grain model of the full length enzyme; residuals are illustrated for the DAMMIN fit; right panel: superimposition of the coarse grain model onto the most representative DAMMIN envelope. c Representation of the scattering curves as Kratky plots for the three individual enzymes Cel48S-t, Cel9A-r and Cel8A-b, indicating their mainly compact and globular shape