Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins.

Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M, Angew Chem Int Ed Engl 56(32):9322-9325 (2017) Europe PMC

SASDCF3 – Nucleolysin TIA-1 isoform p40

Nucleolysin TIA-1 isoform p40
MWI(0) 30 kDa
MWexpected 30 kDa
VPorod 38 nm3
log I(s) 2.30×10-2 2.30×10-3 2.30×10-4 2.30×10-5
Nucleolysin TIA-1 isoform p40 small angle scattering data  s, nm-1
ln I(s)
Nucleolysin TIA-1 isoform p40 Guinier plot ln 2.30×10-2 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleolysin TIA-1 isoform p40 Kratky plot 1.104 0 √3 sRg
p(r)
Nucleolysin TIA-1 isoform p40 pair distance distribution function Rg: 2.9 nm 0 Dmax: 11.2 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of Nucleolysin TIA-1 isoform p40 in 10 mM potassium phosphate, 50 mM NaCl, 10 mM DTT, pH 6 were were collected using a Rigaku BioSAXS-1000 instrument (Munich, Germany) equipped with a Pilatus 100K detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.1542 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.5 and 5 mg/ml were measured at 20°C. Eight successive 7200 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 and the different curves were scaled for protein concentration.

Nucleolysin TIA-1 isoform p40 (TIA-1 wild type)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   30.5 kDa
 
UniProt   P31483-2
Sequence   FASTA