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

SASDYU7 – Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R)

Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R)
MWexperimental 127 kDa
MWexpected 136 kDa
VPorod 166 nm3
log I(s) 1.22×10-2 1.22×10-3 1.22×10-4 1.22×10-5
Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R) small angle scattering data  s, nm-1
ln I(s)
Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R) Guinier plot ln 1.22×10-2 Rg: 4.6 nm 0 (4.6 nm)-2 s2
(sRg)2I(s)/I(0)
Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R) Kratky plot 1.104 0 3 sRg
p(r)
Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R) pair distance distribution function Rg: 5.0 nm 0 Dmax: 17.5 nm

Data validation


There are no models related to this curve.

SAXS data from solutions of Chimeric constructs - CC_1 (AtCel8A_Jo:In-AtCel9R) 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 0.9 and 12.5 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 - CC_1 (AtCel8A_Jo:In-AtCel9R) (AtCel8A_Jo:In-AtCel9)
Mol. type   Protein
Organism   Acetovibrio thermocellus / Streptococcus pneumoniae
Olig. state   Monomer
Mon. MW   136.4 kDa
Sequence   FASTA