| MWexperimental | 590 | kDa |
| MWexpected | 642 | kDa |
| VPorod | 1090 | nm3 |
|
log I(s)
2.51×102
2.51×101
2.51×100
2.51×10-1
|
s, nm-1
|
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 PMCSASDJZ4 – DNA-dependent protein kinase/ X-ray repair cross-complementing protein 5 and 6 complex bound to DNA (DNA-PK monomer )
X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5
DNA-dependent protein kinase catalytic subunit
dsDNA
|
|
|
Fits and models
|
|
|
Synchrotron SAXS
data from solutions of
DNA-dependent protein kinase/ X-ray repair cross-complementing protein 5 and 6 complex bound to DNA (DNA-PK monomer )
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).
In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample
at 5 mg/ml was injected at a 0.25 ml/min flow rate
onto a Shodex KW400 series column
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.
Storage temperature = UNKNOWN. Number of frames = UNKNOWN |
|
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||