Structural characterization of the interaction between BRCA1-BARD1 and RNA polymerase II

Tomas Klumpler.

SASDV58 – BRCA1-associated RING domain protein 1, BRCA1 C-terminus domain (2 mg/ml)

Isoform alpha of BRCA1-associated RING domain protein 1
MWexperimental 22 kDa
MWexpected 26 kDa
VPorod 37 nm3
log I(s) 4.54×10-1 4.54×10-2 4.54×10-3 4.54×10-4
Isoform alpha of BRCA1-associated RING domain protein 1 small angle scattering data  s, nm-1
ln I(s)
Isoform alpha of BRCA1-associated RING domain protein 1 Guinier plot ln 4.54×10-1 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform alpha of BRCA1-associated RING domain protein 1 Kratky plot 1.104 0 √3 sRg
p(r)
Isoform alpha of BRCA1-associated RING domain protein 1 pair distance distribution function Rg: 2.2 nm 0 Dmax: 6.0 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of BRCA1-associated RING domain protein 1, BRCA1 C-terminus domain in 25 mM Tris, 200 mM NaCl, 1 mM DTT, pH 7.9 were collected using a Rigaku BioSAXS-2000 instrument at CEITEC (Brno, Czech Republic) equipped with a HyPix-3000 detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 20°C. One 600 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Isoform alpha of BRCA1-associated RING domain protein 1 (BARD1 BRCT)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   25.6 kDa
 
UniProt   Q99728-2 (535-758)
Sequence   FASTA