| MWexperimental | 20 | kDa |
| MWexpected | 20 | kDa |
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log I(s)
4.98×103
4.98×102
4.98×101
4.98×100
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s, nm-1
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Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein.
Garg A, Orru R, Ye W, Distler U, Chojnacki JE, Köhn M, Tenzer S, Sönnichsen C, Wolf E, J Biol Chem (2019) Europe PMCSASDF47 – Complex of CBP KIX domain with BMAL1 (D530-L625) including C-terminal transactivation domain (TAD) (Mus musculus)
Aryl hydrocarbon receptor nuclear translocator-like protein 1Kinase-inducible domain interacting (KIX) domain of CREB-binding protein (CBP), mutation L664C
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Fits and models
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Synchrotron SAXS
data from solutions of
Complex of CBP KIX domain with BMAL1 (D530-L625) including C-terminal transactivation domain (TAD) (Mus musculus)
in
25 mM Hepes, 150 NaCl, 1 mM DTT, 5% Glycerol, pH 7.2
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).
One solute concentration of 2.58 mg/ml was measured
at 10.4°C.
30 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.
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