Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra.

Franke D, Jeffries CM, Svergun DI, Nat Methods 12(5):419-22 (2015) Europe PMC

SASDA96 – Lysozyme

Lysozyme C
MWI(0) 15 kDa
MWexpected 14 kDa
VPorod 24 nm3
log I(s) 7.79×102 7.79×101 7.79×100 7.79×10-1
Lysozyme C small angle scattering data  s, nm-1
ln I(s)
Lysozyme C Guinier plot ln 7.80×102 Rg: 1.5 nm 0 (1.5 nm)-2 s2
Lysozyme C Kratky plot 1.104 0 3 sRg
Lysozyme C pair distance distribution function Rg: 1.5 nm 0 Dmax: 4.8 nm

Data validation

Fits and models

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

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

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

X-ray synchrotron radiation scattering data from a solution of Lysozyme C in 20 mM Sodium Acetate/HEPES, pH 6.8 were collected on the P12 beam line at Petra-III (Hamburg, Germany) using a Pilatus 2M detector (I(s) vs s, where s = 4π sin θ/λ; 2θ is the scattering angle and λ = 0.12 nm). One solute concentration at 2.61 mg/ml was measured using a total exposure time of 1 second (20 x 0.050 second frames). The data were normalized to the intensity of the transmitted beam and radially averaged. Scattering contributions from the matched solvent blank were subtracted and the resulting 1D scattering data were scaled to protein concentration. The data presented in this entry were obtained from a single concentration scattering curve.

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