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

SASDAD4 – Full length GtBP3

full length CtBP3
MWexperimental 170 kDa
MWexpected 170 kDa
VPorod 330 nm3
log I(s) 2.91×102 2.91×101 2.91×100 2.91×10-1
full length CtBP3 small angle scattering data  s, nm-1
ln I(s)
full length CtBP3 Guinier plot ln 2.92×102 Rg: 5.1 nm 0 (5.1 nm)-2 s2
full length CtBP3 Kratky plot 1.104 0 3 sRg
full length CtBP3 pair distance distribution function Rg: 5.2 nm 0 Dmax: 19 nm

Data validation

Fits and models

log I(s)
 s, nm-1
full length CtBP3 DAMMIN model

log I(s)
 s, nm-1
full length CtBP3 BUNCH model

Synchrotron SAXS data from solutions of Full length GtBP3 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.

full length CtBP3 (full CtBP3)
Mol. type   Protein
Olig. state   Tetramer
Mon. MW   42 kDa
Sequence   FASTA