Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1).

Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J, J Biol Chem 290(5):2644-58 (2015) Europe PMC

SASDCA7 – Ethylene Receptor 1 (DHp + CA domains)

Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains
MWI(0) 25 kDa
MWexpected 55 kDa
VPorod 74 nm3
log I(s) 1.98×101 1.98×100 1.98×10-1 1.98×10-2
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains small angle scattering data  s, nm-1
ln I(s)
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains Guinier plot ln 1.98×101 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains Kratky plot 1.104 0 3 sRg
p(r)
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains pair distance distribution function Rg: 2.8 nm 0 Dmax: 8.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Ethylene Receptor 1 (DHp + CA domains) in 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP, pH 8.8 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 3.1 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 6 mg/ml were measured at 10°C. Eight successive 15 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 low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Tags: X33
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains (ETR1_DHp-CA)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Dimer
Mon. MW   27.5 kDa
 
UniProt   P49333 (339-589)
Sequence   FASTA