| MWI(0) | 76 | kDa |
| MWexpected | 76 | kDa |
| VPorod | 130 | nm3 |
|
log I(s)
1.83×102
1.83×101
1.83×100
1.83×10-1
|
s, nm-1
|
Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.
Márquez JA, Smith CI, Petoukhov MV, Lo Surdo P, Mattsson PT, Knekt M, Westlund A, Scheffzek K, Saraste M, Svergun DI, EMBO J 22(18):4616-24 (2003) Europe PMCSASDC52 – Bruton tyrosine kinase
Tyrosine-protein kinase BTK (R28C mutant)|
|
|
Fits and models
|
|
|
|
|
Synchrotron SAXS data from solutions of Brutons's tyrosine kinase (Btk) in 20 mM HEPES, 200 mM NaCl, 2 mM DTT, 1 mM MgCl2, pH 7.5, were collected on the X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a 1D Gas detector detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Solute concentrations ranging between 1 and 10 mg/ml were measured at 10°C. 15 successive 60 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 and the different curves were scaled for protein concentration. 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 Guinier range is very short subject to experimental conditions
Tags:
X33
|
|
|||||||||||||||||||||||||||