| MWI(0) | 41 | kDa |
| MWexpected | 47 | kDa |
| VPorod | 69 | nm3 |
|
log I(s)
1.00×104
1.00×103
1.00×102
1.00×101
|
s, nm-1
|
Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase.
Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O, Nat Commun 8(1):2101 (2017) Europe PMCSASDC26 – DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210
BCR-ABL p210 fusion protein (DH-PH)|
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Fits and models
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Rg, nm
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Synchrotron SAXS
data from solutions of
DH-PH - Dbl-homology domain (DH) and Pleckstrin-homology (PH) of Bcr-Abl tyrosine kinase p210
in
25 mM Tris-HCl, 150 mM NaCl, 5% Glycerol, 1 mM DTT, pH 7.5
were collected
on the
EMBL P12 beam line
at the PETRA III storage ring
(DESY; Hamburg, Germany)
using a Pilatus 2M detector
at a sample-detector distance of 3 m and
at a wavelength of λ = 0.124 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 1.8 and 14.4 mg/ml were measured
at 20°C.
20 successive
0.045 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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