Inhibitor-induced dimerization of an essential oxidoreductase from African Trypanosomes.

Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA, Angew Chem Int Ed Engl (2019) Europe PMC

SASDEZ3 – Tryparedoxin, oxidized state

MWexperimental 16 kDa
MWexpected 16 kDa
VPorod 27 nm3
log I(s) 1.06×101 1.06×100 1.06×10-1 1.06×10-2
Tryparedoxin small angle scattering data  s, nm-1
ln I(s)
Tryparedoxin Guinier plot ln 1.07×101 Rg: 1.6 nm 0 (1.6 nm)-2 s2
Tryparedoxin Kratky plot 1.104 0 3 sRg
Tryparedoxin pair distance distribution function Rg: 1.6 nm 0 Dmax: 6.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Tryparedoxin GASBOR model

log I(s)
 s, nm-1
Tryparedoxin CORAL model

log I(s)
 s, nm-1
Tryparedoxin PDB (PROTEIN DATA BANK) model
Tryparedoxin OTHER model

Synchrotron SAXS data from solutions of Tryparedoxin, oxidized state, in 10 mM HEPES pH 7.5, 50 mM NaCl, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Dectris Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). The data were collected using in-line size exclusion chromatography (SEC)-SAXS at 20°C.

SEC column type: GE Healthcare S75 3.2/300; Sample Injection Concentration = 10 mg/mL; Column flow-rate = 0.1 mL/min.

Mol. type   Protein
Organism   Trypanosoma brucei brucei
Olig. state   Monomer
Mon. MW   15.8 kDa
UniProt   O77404
Sequence   FASTA