Unique Structural Features of Mammalian NEIL2 DNA Glycosylase Prime Its Activity for Diverse DNA Substrates and Environments.

Eckenroth BE, Cao VB, Averill AM, Dragon JA, Doublié S, Structure (2020) Europe PMC

SASDJB4 – Endonuclease VIII - Like 2 from Monodelphis domestica (size exclusion chromatography SAXS) full length

Nei like DNA glycosylase 2
MWI(0) 44 kDa
MWexpected 39 kDa
VPorod 58 nm3
log I(s) 1.85×102 1.85×101 1.85×100 1.85×10-1
Nei like DNA glycosylase 2 small angle scattering data  s, nm-1
ln I(s)
Nei like DNA glycosylase 2 Guinier plot ln 1.86×102 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Nei like DNA glycosylase 2 Kratky plot 1.104 0 √3 sRg
p(r)
Nei like DNA glycosylase 2 pair distance distribution function Rg: 2.7 nm 0 Dmax: 8.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Endonuclease VIII - Like 2 from Monodelphis domestica (size exclusion chromatography SAXS) full length in 25 mM Bis-Tris, 150 mM NaCl, 2% glycerol, 1 mM TCEP, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a wavelength of λ = 0.103 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 70.00 μl sample at 5 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample detector distance = UNKNOWN. Number of frames = UNKNOWN

Nei like DNA glycosylase 2 (MdoNEIL2)
Mol. type   Protein
Organism   Monodelphis domestica
Olig. state   Monomer
Mon. MW   39.0 kDa
 
UniProt   F7AMK3 (3-336)
Sequence   FASTA