Integrative SAXS and AFM analysis of engineered carbohydrate-active enzyme assemblies with tunable spatial organization.

Pardo Larrabeiti I, Eibinger M, Esque J, Pradeau S, Fort S, Moraïs S, Mizrahi I, Bayer EA, Nidetzky B, Montanier CY, Roblin P, Dumon C, Protein Sci 35(7):e70649 (2026) Europe PMC

SASDYZ7 – Chimeric constructs - XCC_F (AtCel9R-Jo-AtCel8A:In-AtXyn11A)

Chimeric constructs - XCC
MWexperimental 205 kDa
MWexpected 175 kDa
log I(s) 1.52×10-4 1.52×10-5 1.52×10-6 1.52×10-7
Chimeric constructs - XCC small angle scattering data  s, nm-1
ln I(s)
Chimeric constructs - XCC Guinier plot ln 1.52×10-4 Rg: 5.4 nm 0 (5.4 nm)-2 s2
(sRg)2I(s)/I(0)
Chimeric constructs - XCC Kratky plot 1.104 0 √3 sRg
p(r)
Chimeric constructs - XCC pair distance distribution function Rg: 5.5 nm 0 Dmax: 18.4 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of Chimeric constructs - XCC_F (AtCel9R-Jo-AtCel8A:In-AtXyn11A) in 25 mM Tris, 150 mM NaCl, pH 8 were collected on the XEUSS 2.0 instrument (Laboratoire de Génie Chimique, Toulouse, France) using a Pilatus 1M detector (DECTRIS, Switzerland) detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1.7 and 14.7 mg/ml were measured at 20°C. 12 successive 600 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Chimeric constructs - XCC (XCC-F)
Mol. type   Protein
Olig. state   Monomer
Mon. MW   174.8 kDa
Sequence   FASTA