Domain deletion constructs of hHR23B

Sarasi Galagedera.

SASDSN6 – Human full length RAD23B

UV excision repair protein RAD23 homolog B
MWI(0) 43 kDa
MWexpected 43 kDa
VPorod 103 nm3
log I(s) 1.67×10-2 1.67×10-3 1.67×10-4 1.67×10-5
UV excision repair protein RAD23 homolog B small angle scattering data  s, nm-1
ln I(s)
UV excision repair protein RAD23 homolog B Guinier plot ln 1.68×10-2 Rg: 4.6 nm 0 (4.6 nm)-2 s2
(sRg)2I(s)/I(0)
UV excision repair protein RAD23 homolog B Kratky plot 1.104 0 √3 sRg
p(r)
UV excision repair protein RAD23 homolog B pair distance distribution function Rg: 5.2 nm 0 Dmax: 26 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Human full length RAD23B in 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH 6.8 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory storage ring (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.1033 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 300.00 μl sample at 2.8 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20°C. 21 successive 0.500 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.

UV excision repair protein RAD23 homolog B (hHR23B)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   43.2 kDa
 
UniProt   P54727 (1-409)
Sequence   FASTA