NSRRC TPS13A standard protein archive

Orion Shih.

SASDRM8 – Lysozyme C (Gallus gallus)

Lysozyme C
MWexperimental 11 kDa
MWexpected 14 kDa
VPorod 13 nm3
log I(s) 8.95×10-2 8.95×10-3 8.95×10-4 8.95×10-5
Lysozyme C small angle scattering data  s, nm-1
ln I(s)
Lysozyme C Guinier plot ln 8.96×10-2 Rg: 1.4 nm 0 (1.4 nm)-2 s2
(sRg)2I(s)/I(0)
Lysozyme C Kratky plot 1.104 0 3 sRg
p(r)
Lysozyme C pair distance distribution function Rg: 1.4 nm 0 Dmax: 4.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of lysozyme in 40 mM sodium acetate, 50 mM NaCl, pH 4 were collected on the 13A beam line at the Taiwan Photon Source (NSRRC, Hsinchu, Taiwan) using a Eiger X 1M and Eiger X 9M detector at a sample-detector distance of 2.4 m and at a wavelength of λ = 0.083 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 10 mg/ml was injected at a 0.35 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 10°C. Six successive 2 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.

SAXS data shows influence of repulsive interparticle interference.

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