|
Synchrotron SAXS
data from solutions of
Schistosoma mansoni Venom Allergen-like protein isoform 11 (SmVAL11) - Cleaved domains
in
25 mM MES, 125 mM NaCl, 1 mM EDTA, pH 6.8
were collected
on the
SWING beam line
at the SOLEIL storage ring
(Saint-Aubin, France)
using a Eiger 4M detector
at a sample-detector distance of 2 m and
at a wavelength of λ = 0.76 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 45.00 μl sample
at 11 mg/ml was injected at a 0.30 ml/min flow rate
onto a Cytiva Superdex 200 Increase 3.2/300 column
at 20°C.
2400 successive
1 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.
SmVAL11 is a 45 kDa protein containing two SCP/TAPS domains arranged in tandem and connected by a flexible linker. The protein is prone to autocleavage at the linker region, resulting in a heterogeneous sample containing multiple species in solution. To address this, SAXS measurements were coupled to Size Exclusion Chromatography (SEC-SAXS) to separate and individually analyse the different populations.
The scattering data presented here were obtained by Evolving Factor Analysis (EFA) deconvolution of the 2nd most intense elution peak, as implemented in RAW, and likely correspond to the cleaved domains of SmVAL11 protein.
|
|
s, nm-1
