Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site

Al Kikhney, Marco Salomone-Stagni.

SASDAL7 – Metal-free hETHE1, 3 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial
MWexperimental 828 kDa
MWexpected 56 kDa
VPorod 1445 nm3
log I(s) 3.18×102 3.18×101 3.18×100 3.18×10-1
Persulfide dioxygenase ETHE1, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Persulfide dioxygenase ETHE1, mitochondrial Guinier plot ln 3.19×102 Rg: 11.2 nm 0 (11.2 nm)-2 s2
(sRg)2I(s)/I(0)
Persulfide dioxygenase ETHE1, mitochondrial Kratky plot 1.104 0 √3 sRg
p(r)
Persulfide dioxygenase ETHE1, mitochondrial pair distance distribution function Rg: 14.1 nm 0 Dmax: 56 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Persulfide dioxygenase ETHE1, mitochondrial DAMMIN model
Synchrotron SAXS data from solutions of Metal-free hETHE1, 3 mg/ml in 50 mM Tris 150 mM NaCl 2 mM TCEP, pH 8 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (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 5°C. Four successive 30 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.

Storage temperature = UNKNOWN

Tags: X33
Persulfide dioxygenase ETHE1, mitochondrial (hETHE1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   27.9 kDa
 
UniProt   O95571