Cryo-EM led analysis of open and closed conformations of Chagas vaccine candidate TcPOP.

Batra S, Olmo F, Ragan TJ, Kaplan M, Calvaresi V, Frank AM, Lancey C, Assadipapari M, Ying C, Struwe WB, Hesketh EL, Kelly JM, Barfod L, Campeotto I, Nat Commun 16(1):7164 (2025) Europe PMC

SASDW33 – STATIC-SAXS of Trypanosoma cruzi Prolyl Oligopepetidase (TcPOP)

Prolyl endopeptidase
MWI(0) 106 kDa
MWexpected 78 kDa
VPorod 170 nm3
log I(s) 4.17×10-2 4.17×10-3 4.17×10-4 4.17×10-5
Prolyl endopeptidase small angle scattering data  s, nm-1
ln I(s)
Prolyl endopeptidase Guinier plot ln 4.17×10-2 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Prolyl endopeptidase Kratky plot 1.104 0 3 sRg
p(r)
Prolyl endopeptidase pair distance distribution function 0 Dmax: 0.0 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of STATIC-SAXS of Trypanosoma cruzi Prolyl Oligopepetidase (TcPOP) in 20 mM HEPES, 150 mM NaCl, pH 7.4 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 3.7 m and at a wavelength of λ = 0.09464 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 6 mg/ml were measured at 15°C. 21 successive 1 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.

CAUTION! Data are severely over subtracted. CAUTION! Severe aggregation. CAUTION! The Rg, I(0), particle size/volume, molecular weight, p(r) and any other structural parameters derived from the data are undefined/uninterpretable.

Prolyl endopeptidase
Mol. type   Protein
Organism   Trypanosoma cruzi
Olig. state   Monomer
Mon. MW   78.3 kDa
 
UniProt   Q71MD6
Sequence   FASTA