| MWexperimental | 40 | kDa |
| MWexpected | 38 | kDa |
| VPorod | 53 | nm3 |
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log I(s)
7.62×101
7.62×100
7.62×10-1
7.62×10-2
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s, nm-1
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Beyond the VSG Layer: Exploring the Role of Intrinsic Disorder in the Invariant Surface Glycoproteins of African Trypanosomes.
Sülzen H, Volkov AN, Geens R, Zahedifard F, Stijlemans B, Zoltner M, Magez S, Sterckx YG, Zoll S, PLoS Pathog 20(4):e1012186 (2024) Europe PMCSASDT75 – Trypanosoma brucei gambiense invariant surface glycoprotein 43 (ISG43)
T. brucei spp.-specific protein|
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Fits and models
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Synchrotron SAXS
data from solutions of
Trypanosoma brucei gambiense invariant surface glycoprotein 43 (ISG43)
in
20 mM HEPES, 150 mM NaCl, 3% glycerol, pH 7.5
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 = 0.099 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 50.00 μl sample
at 10.0 mg/ml was injected at a 0.20 ml/min flow rate
onto a Shodex KW404-4F column
at 20°C.
1000 successive
0.750 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.
For display purposes the SAXS intensities have been scaled to the model-fit data (I(s) multiplied by 1000000000). |
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