| MWexperimental | 44 | kDa |
| MWexpected | 45 | kDa |
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log I(s)
1.55×10-2
1.55×10-3
1.55×10-4
1.55×10-5
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s, nm-1
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Conformational ensembles of flexible multidomain proteins: How close are we to accurate and reliable predictions?
Rodriguez S Fournet A, Bartels S, Pajkos M, Clerc I, Carrière L, Thureau A, Montanier C, Dumon C, Allemand F, Cortés J, Bernadó P, Biophysical Journal (2026) DOISASD268 – Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 18
Glycosyl hydrolase (GH) linked to a Carbohydrate-binding module (CBM) 18|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
Conformational ensembles of domain–linker–domain (DLD) protein chimera consisting of Glycosyl hydrolase and Carbohydrate binding module 18
in
50 mM Na-phosphate, 2 mM TCEP, pH 6
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 = 0.103 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 8.4 mg/ml was injected at a 0.20 ml/min flow rate
onto a column
at 15°C.
630 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.
All 50 conformers were refined using MoMa FReSa, which is available as an additional zipped file. |
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