| MWI(0) | 16 | kDa |
| MWexpected | 22 | kDa |
| VPorod | 38 | nm3 |
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log I(s)
2.07×103
2.07×102
2.07×101
2.07×100
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s, nm-1
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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 PMCSASDC46 – PH - Pleckstrin-homology domain of Bcr-Abl tyrosine kinase p210
BCR-ABL p210 fusion protein (PH domain)|
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Fits and models
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Synchrotron SAXS
data from solutions of
PH - Pleckstrin-homology domain 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 and 9.1 mg/ml were measured
at 10°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.
The homology model is derived from PDB ID: 2z0q. The PDB entry for BCR-ABL p210 fusion protein PH domain is 5oc7 (has an internal deletion). |
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