E3 ubiquitin/ISG15 ligase TRIM25

Kevin Haubrich.

SASDKA8 – E3 ubiquitin/ISG15 ligase TRIM25 bound to lnczc3h7a_304-326 RNA (TRIM25/lnczc3h7a)

E3 ubiquitin/ISG15 ligase TRIM25
lnczc3h7a_304-326
MWexperimental 101 kDa
MWexpected 108 kDa
log I(s) 3.26×10-2 3.26×10-3 3.26×10-4 3.26×10-5
E3 ubiquitin/ISG15 ligase TRIM25 lnczc3h7a_304-326 small angle scattering data  s, nm-1
ln I(s)
E3 ubiquitin/ISG15 ligase TRIM25 lnczc3h7a_304-326 Guinier plot ln 3.27×10-2 Rg: 5.8 nm 0 (5.8 nm)-2 s2
(sRg)2I(s)/I(0)
E3 ubiquitin/ISG15 ligase TRIM25 lnczc3h7a_304-326 Kratky plot 1.104 0 3 sRg
p(r)
E3 ubiquitin/ISG15 ligase TRIM25 lnczc3h7a_304-326 pair distance distribution function Rg: 5.6 nm 0 Dmax: 16.6 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of TRIM25/lnczc3h7a in 20 mM MES, 75 mM NaCl, 1 mM TCEP, pH 6.5 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 20 successive 0.050 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.

The concentration estimate quoted for this entry is likely inaccurate due to the uncertainty of the complex's molar extinction coefficient (protein plus RNA).

E3 ubiquitin/ISG15 ligase TRIM25 (TRIM25)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   50.1 kDa
 
UniProt   Q14258 (189-630)
Sequence   FASTA
 
lnczc3h7a_304-326 (lnczc3h7a-SL)
Mol. type   RNA
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   8.3 kDa
Sequence   FASTA