Reconstitution of the DTX3L-PARP9 complex reveals determinants for high affinity heterodimerization and multimeric assembly.

Ashok Y, Vela-Rodríguez C, Yang CS, Alanen HI, Liu F, Paschal BM, Lehtiö L, Biochem J (2022) Europe PMC

SASDMQ6 – The N-terminus of E3 ubiquitin-protein ligase DTX3L (M1-Q200)

E3 ubiquitin-protein ligase DTX3L
MWexperimental 121 kDa
MWexpected 114 kDa
VPorod 200 nm3
log I(s) 1.71×10-1 1.71×10-2 1.71×10-3 1.71×10-4
E3 ubiquitin-protein ligase DTX3L small angle scattering data  s, nm-1
ln I(s)
E3 ubiquitin-protein ligase DTX3L Guinier plot ln 1.71×10-1 Rg: 4.7 nm 0 (4.7 nm)-2 s2
(sRg)2I(s)/I(0)
E3 ubiquitin-protein ligase DTX3L Kratky plot 1.104 0 3 sRg
p(r)
E3 ubiquitin-protein ligase DTX3L pair distance distribution function Rg: 4.7 nm 0 Dmax: 17 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the N-terminus of E3 ubiquitin-protein ligase DTX3L in 30 mM HEPES, 350 mM NaCl, 10% glycerol, 0.5 mM TCEP, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Pilatus 2M detector at a wavelength of λ = 0.1 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 60.00 μl sample was injected at a 0.06 ml/min flow rate onto a GE Superose 6 Increase 3.2/300 column at 24.8°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

E3 ubiquitin-protein ligase DTX3L (DTX3L)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Pentamer
Mon. MW   22.8 kDa
 
UniProt   Q8TDB6 (1-200)
Sequence   FASTA