Deciphering the structural insights and concentration-dependent dimerisation of endo-β-1,4-xylanase (AcXyn30B_12) from Acetivibrio clariflavus using SAXS and computational methods.

Choudhury B, Goyal A, FEBS J (2026) Europe PMC

SASDYN2 – endo-β-1,4-xylanase (AcXyn30B_12) from Acetivibrio clariflavus

endo-β-1,4-xylanase (AcXyn30B_12)
MWexperimental 73 kDa
MWexpected 74 kDa
log I(s) 1.16×105 1.16×104 1.16×103 1.16×102
endo-β-1,4-xylanase (AcXyn30B_12) small angle scattering data  s, nm-1
ln I(s)
endo-β-1,4-xylanase (AcXyn30B_12) Guinier plot ln 1.17×105 Rg: 4 nm 0 (4 nm)-2 s2
(sRg)2I(s)/I(0)
endo-β-1,4-xylanase (AcXyn30B_12) Kratky plot 1.104 0 3 sRg

Data validation


There are no models related to this curve.

SAXS data from solutions of endo-β-1,4-xylanase (AcXyn30B_12) from Acetivibrio clariflavus in 50 mM Sodium Phosphate, pH 7.5 were collected on the Anton Paar SAXSpace instrument (Medical University of Graz, Graz, Austria) using a Roper Scientific PI-SCX:4300 detector at a sample-detector distance of 1 m and at a wavelength of λ = 1.54 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

CAUTION: The reported experimental uncertainties appear inconsistent with the variation in the data, preventing a clear identification of the Guinier region. Derived parameters should be interpreted with caution

endo-β-1,4-xylanase (AcXyn30B_12) (AcXyn30B_12)
Mol. type   Protein
Organism   Acetivibrio clariflavus
Olig. state   Monomer
Mon. MW   73.5 kDa
Sequence   FASTA