| MWexperimental | 170 | kDa |
| MWexpected | 171 | kDa |
| VPorod | 280 | nm3 |
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log I(s)
1.51×103
1.51×102
1.51×101
1.51×100
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s, nm-1
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Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM.
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA, Prog Biophys Mol Biol (2020) Europe PMCSASDJW4 – X-ray repair cross-complementing proteins 5 and 6-DNA
X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5
Y-DNA
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Fits and models
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Synchrotron SAXS
data from solutions of
X-ray repair cross-complementing proteins 5 and 6-DNA
in
50 mM Tris-HCl, 100 mM NaCl, 5% glycerol, 0.01% sodium azide, pH 7.5
were collected
on the
12.3.1 (SIBYLS) beam line
at the Advanced Light Source (ALS) storage ring
(Berkeley, CA, USA)
using a MAR 165 CCD detector
at a sample-detector distance of 1.5 m and
at a wavelength of λ = 0.103 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 20°C.
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.
Storage temperature = UNKNOWN. Number of frames = UNKNOWN |
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