| MWI(0) | 45 | kDa |
| MWexpected | 14 | kDa |
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log I(s)
3.96×101
3.96×100
3.96×10-1
3.96×10-2
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s, nm-1
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Self-assembly and conformational heterogeneity of the AXH domain of ataxin-1: an unusual example of a chameleon fold.
de Chiara C, Rees M, Menon RP, Pauwels K, Lawrence C, Konarev PV, Svergun DI, Martin SR, Chen YW, Pastore A, Biophys J 104(6):1304-13 (2013) Europe PMCSASDL47 – Oligomeric composition of AXH Domain of Ataxin-1 (wild type and A567G, I580A mutants)
Ataxin-1|
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Fits and models
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Synchrotron SAXS
data from solutions of
Oligomeric composition of AXH Domain of Ataxin-1 (wild type and A567G, I580A mutants)
in
20 mM Tris-HCl, pH 7
were collected
on the
EMBL X33 beam line
at the DORIS III, DESY storage ring
(Hamburg, Germany)
using a Pilatus 1M-W detector
at a sample-detector distance of 2.7 m and
at a wavelength of λ = 0.154 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 9.30 mg/ml was measured
at 10°C.
Eight successive
15 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.
OLIGOMER analysis of concentration series data, including models and fits, are made available in the full entry zip archive for the wild-type, A567G and I580A mutant variants of the protein.
Tags:
X33
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