TIA-1 RRM23 binding and recognition of target oligonucleotides.

Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA, Nucleic Acids Res 45(8):4944-4957 (2017) PubMed

SASDBM6 – Nucleolysin TIA-1 isoform p40

Nucleolysin TIA-1 isoform p40
MWexperimental 20 kDa
MWexpected 21 kDa
VPorod 26 nm3
log I(s) 3.40×10-2 3.40×10-3 3.40×10-4 3.40×10-5
Nucleolysin TIA-1 isoform p40 small angle scattering data  s, nm-1
ln I(s)
Nucleolysin TIA-1 isoform p40 Guinier plot ln 3.40×10-2 Rg: 2.3 nm 0 (2.3 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: 2.5 nm 0 Dmax: 8.8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from a solution of nucleolysin TIA-1 (isoform p40; amino acids 93-274) in 20 mM HEPES, 100mM NaCl, 3% v/v glycerol, pH 7, were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.6 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). The data were collected as 30 successive 1 second frames and were normalized to the intensity of the transmitted beam and radially averaged. The radially-averaged scattering of the solvent-blank was subtracted to produce the results displayed in this entry that shows the scattering profile from a sample at 2.5 mg/ml maintained at 15°C during the SAXS measurements.

Apo-TIA-1 RRM23

Nucleolysin TIA-1 isoform p40 (TIA-1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   21.3 kDa
 
UniProt   p31483-2 (93-274)
Sequence   FASTA