The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured.

Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M, Protein Sci 15(5):1042-50 (2006) Europe PMC

SASDAE4 – C-terminal CtBP3

C-term part CtBP3
MWexperimental 56 kDa
MWexpected 52 kDa
VPorod 126 nm3
log I(s) 1.05×104 1.05×103 1.05×102 1.05×101
C-term part CtBP3 small angle scattering data  s, nm-1
ln I(s)
C-term part CtBP3 Guinier plot ln 1.05×104 Rg: 5.5 nm 0 (5.5 nm)-2 s2
(sRg)2I(s)/I(0)
C-term part CtBP3 Kratky plot 1.104 0 3 sRg
p(r)
C-term part CtBP3 pair distance distribution function Rg: 5.6 nm 0 Dmax: 20 nm

Data validation


Fits and models


log I(s)
 s, nm-1
C-term part CtBP3 DAMMIN model

log I(s)
 s, nm-1
C-term part CtBP3 BUNCH model

Synchrotron SAXS data from solutions of C-terminal CtBP3 in 25 mM Tris/HCl 250 mM NaCl, pH 8 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2 and 8 mg/ml were measured at 10°C. Two successive 120 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.

C-term part CtBP3 (C-term CtBP3)
Mol. type   Protein
Olig. state   Dimer
Mon. MW   26.5 kDa
Sequence   FASTA