SWING_20221204

Franck COSTE.

SASDRA8 – The BTB domain (S103R mutant) of the zinc finger and BTB domain-containing protein 8A.1-A (ZBTB8a) from Xenopus laevis

Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant)
MWexperimental 40 kDa
MWexpected 35 kDa
VPorod 60 nm3
log I(s) 6.16×10-2 6.16×10-3 6.16×10-4 6.16×10-5
Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) small angle scattering data  s, nm-1
ln I(s)
Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) Guinier plot ln 6.17×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) Kratky plot 1.104 0 3 sRg
p(r)
Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant) pair distance distribution function Rg: 3.3 nm 0 Dmax: 12.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the BTB domain (S103R mutant) from ZBTB8a in 20 mM Hepes, 150 mM NaCl, 0.5 mM TCEP, pH 7.5 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.103316 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 10 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 630 successive 0.990 second frames were collected through the SEC elution. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Possibly aggregated.

Zinc finger and BTB domain-containing protein 8A.1-A (S103R mutant)
Mol. type   Protein
Organism   Xenopus laevis
Olig. state   Dimer
Mon. MW   17.6 kDa
 
UniProt   Q0IH98 (1-147)
Sequence   FASTA