Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme.

Ashish, J Biomol Struct Dyn :1-15 (2021) Europe PMC

SASDMH2 – SAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-2.75 1/nm

Lysozyme C
MWexperimental 14 kDa
MWexpected 14 kDa
log I(s) 2.47×102 2.47×101 2.47×100 2.47×10-1
Lysozyme C small angle scattering data  s, nm-1
ln I(s)
Lysozyme C Guinier plot ln 2.47×102 Rg: 1.4 nm 0 (1.4 nm)-2 s2
Lysozyme C Kratky plot 1.104 0 3 sRg
Lysozyme C pair distance distribution function Rg: 1.4 nm 0 Dmax: 4.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Lysozyme C DAMMIF model
Lysozyme C DAMFILT model
Lysozyme C OTHER model

log I(s)
 s, nm-1
Lysozyme C SREFLEX model

log I(s)
 s, nm-1
Lysozyme C PDB (PROTEIN DATA BANK) model

Synchrotron SAXS data from solutions lysozyme in 40 mM NaOAc pH 3.8, 150 mM NaCl, pH 3.8 were collected on the X9A beam line at the National Synchrotron Light Source (NSLS) storage ring (Brookhaven, NY, USA) using a Pilatus 300K detector at a wavelength of λ = 0.129 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.9 and 5 mg/ml were measured at 10°C. Three successive 30 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.

Please refer to publication entitled same as this project for details on how this dataset was generated by averaging concentration series.

Lysozyme C (Lysozyme, lys)
Mol. type   Protein
Organism   Gallus gallus
Olig. state   Monomer
Mon. MW   14.3 kDa
UniProt   P00698 (19-147)
Sequence   FASTA