| MWI(0) | 250 | kDa |
| MWexpected | 323 | kDa |
| VPorod | 312 | nm3 |
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log I(s)
2.30×102
2.30×101
2.30×100
2.30×10-1
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s, nm-1
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A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex.
Sterckx YG, JovĂ© T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R, J Mol Biol 428(8):1589-603 (2016) Europe PMCSASDAA9 – EcPaaA2-EcParE2His construct
Plasmid stabilization protein ParEUncharacterized protein (Antitoxin)
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Fits and models
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Synchrotron SAXS
data from solutions of
EcPaaA2-EcParE2His construct
in
50 mM Tris-HCl 500 mM NaCl, pH 7.5
were collected
on the
BM29 beam line
at the ESRF storage ring
(Grenoble, France)
using a Pilatus 1M detector
at a sample-detector distance of 2.4 m and
at a wavelength of λ = 0.093 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 0.5 and 3.5 mg/ml were measured
at 10°C.
10 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.
The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Use of SAXS to validate the oligomer state of the obtained crystal structure and to model missing afinity tags |
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