| MWexperimental | 177 | kDa |
| MWexpected | 178 | kDa |
| VPorod | 305 | nm3 |
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log I(s)
2.45×10-2
2.45×10-3
2.45×10-4
2.45×10-5
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s, nm-1
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Post-translational acylation drives folding and activity of the CyaA bacterial toxin
Corentin Léger.SASDXH6 – Adenylate Cyclase Toxine proCyaA
Adenylate cyclase Toxin|
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Fits and models
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Synchrotron SAXS
data from solutions of
Adenylate Cyclase Toxine proCyaA
in
20mM HEPES , 50mM NaCl, 2mM CaCl2, pH 7.4
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 4 m and
at a wavelength of λ = 0.1033 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 1.0 and 2.9 mg/ml were measured
at 15°C.
20 successive
0.990 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.
The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
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