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

SASDEG4 – Tryparedoxin K102E, oxidized state

Tryparedoxin K102E
MWexperimental 15 kDa
MWexpected 16 kDa
VPorod 26 nm3
log I(s) 8.01×100 8.01×10-1 8.01×10-2 8.01×10-3
Tryparedoxin K102E small angle scattering data  s, nm-1
ln I(s)
Tryparedoxin K102E Guinier plot ln 8.01×100 Rg: 1.6 nm 0 (1.6 nm)-2 s2
Tryparedoxin K102E Kratky plot 1.104 0 3 sRg
Tryparedoxin K102E pair distance distribution function Rg: 1.5 nm 0 Dmax: 4.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Tryparedoxin K102E PDB (PROTEIN DATA BANK) model
Tryparedoxin K102E OTHER model

Synchrotron SAXS data from solutions of Tryparedoxin K102E, 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.

Tryparedoxin K102E
Mol. type   Protein
Organism   Trypanosoma brucei brucei
Olig. state   Monomer
Mon. MW   15.8 kDa
UniProt   O77404
Sequence   FASTA