Human APE1-DNA Ligase1 complex in the presence of DNA

farheen jahan.

SASDVH6 – Human DNA repair nuclease/redox regulator APEX1 (APE-1/APEX-1) bound to DNA ligase-1

DNA ligase 1
DNA repair nuclease/redox regulator APEX1
MWexperimental 138 kDa
MWexpected 137 kDa
VPorod 289 nm3
log I(s) 1.27×102 1.27×101 1.27×100 1.27×10-1
DNA ligase 1 DNA repair nuclease/redox regulator APEX1 small angle scattering data  s, nm-1
ln I(s)
DNA ligase 1 DNA repair nuclease/redox regulator APEX1 Guinier plot ln 1.28×102 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
DNA ligase 1 DNA repair nuclease/redox regulator APEX1 Kratky plot 1.104 0 3 sRg
p(r)
DNA ligase 1 DNA repair nuclease/redox regulator APEX1 pair distance distribution function Rg: 5.2 nm 0 Dmax: 15.0 nm

Data validation


Fits and models


log I(s)
 s, nm-1
DNA ligase 1 DNA repair nuclease/redox regulator APEX1 DAMFILT model

Synchrotron SAXS data from solutions of DNA repair nuclease/redox regulator APEX1 (APE-1/APEX-1) bound to DNA ligase-1 in 50 mM Tris pH 7.5, 200 mM NaCl, 2% glycerol were collected on the BL-18 beam line at the INDUS-2 (Indore, India) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 25°C. Two successive 1800 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.

CAUTION: Dmax underestimated. CAUTION: Likely inconsistency in background subtraction. Note: X-ray wavelength= UNKNOWN. Note: Sample to detector distance = UNKNOWN. Note: The model displayed in this entry is derived from the spatial alignment of an individual model cohort consisting of several different models where the aligned models have undergone subsequent volume and bead-occupancy correction (DAMFILT). Consequently, the model displayed in this entry is in no way related to the displayed fit to the data.

DNA ligase 1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   101.7 kDa
Sequence   FASTA
 
DNA repair nuclease/redox regulator APEX1
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   35.6 kDa
 
UniProt   P27695 (1-318)
Sequence   FASTA