KDSAXS: A tool for Analyzing Binding Equilibria with SAXS Data using Explicit Models

Gomes T, Ruiz L, Martin-Malpartida P, Bernadó P, Baptista A, Macias M, Cordeiro T, Journal of Molecular Biology :169103 (2025) DOI

SASDWP8 – β-Lactoglobulin A at 26.1 µM (pH 7.0)

Beta-lactoglobulin
MWexperimental 10 kDa
MWexpected 20 kDa
VPorod 30 nm3
log I(s) 5.58×100 5.58×10-1 5.58×10-2 5.58×10-3
Beta-lactoglobulin small angle scattering data  s, nm-1
ln I(s)
Beta-lactoglobulin Guinier plot ln 5.58×100 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
Beta-lactoglobulin Kratky plot 1.104 0 3 sRg
Dmax: 8.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of β-Lactoglobulin A at 26.1 µM (pH 7.0) in 20 mM MOPS, 100 mM NaCl, 1 mM TCEP were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.0999 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 0.48 mg/ml was measured at 20°C. 20 successive 0.500 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.

Beta-lactoglobulin (BLG A)
Mol. type   Protein
Organism   Bos taurus
Olig. state   Unknown
Mon. MW   19.9 kDa
 
UniProt   P02754 (1-178)
Sequence   FASTA