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

SASDCC3 – Nucleolysin TIA-1 isoform p40 in complex with U15 RNA

Nucleolysin TIA-1 isoform p40
poly U 15mer
MWI(0) 47 kDa
MWexpected 35 kDa
VPorod 39 nm3
log I(s) 3.59×10-2 3.59×10-3 3.59×10-4 3.59×10-5
Nucleolysin TIA-1 isoform p40 poly U 15mer small angle scattering data  s, nm-1
ln I(s)
Nucleolysin TIA-1 isoform p40 poly U 15mer Guinier plot ln 3.60×10-2 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleolysin TIA-1 isoform p40 poly U 15mer Kratky plot 1.104 0 √3 sRg
p(r)
Nucleolysin TIA-1 isoform p40 poly U 15mer pair distance distribution function Rg: 2.4 nm 0 Dmax: 8.7 nm

Data validation

There are no models related to this curve.

SAXS data from solutions of Nucleolysin TIA-1 isoform p40 in complex with U15 RNA in 10 mM potassium phosphate, 50 mM NaCl, 10 mM DTT, pH 6 were collected using a Rigaku BioSAXS-1000 instrument (Munich, Germany) equipped with a Pilatus 100K detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). X-ray wavelength = unknown Sample-to-detector distance = unknown Sample concentration(s) = unknown

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

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
 
poly U 15mer (U15)
Mol. type   RNA
Olig. state   Monomer
Mon. MW   4.6 kDa
Sequence   FASTA