Structural and molecular comparison of bacterial and eukaryotic trigger factors.

Ries F, Carius Y, Rohr M, Gries K, Keller S, Lancaster CRD, Willmund F, Sci Rep 7(1):10680 (2017) Europe PMC

SASDX22 – chloroplast trigger factor from Chlamydomonas reinhardtii

peptidylprolyl isomerase
MWexperimental 49 kDa
MWexpected 54 kDa
VPorod 103 nm3
log I(s) 5.18×101 5.18×100 5.18×10-1 5.18×10-2
peptidylprolyl isomerase small angle scattering data  s, nm-1
ln I(s)
peptidylprolyl isomerase Guinier plot ln 5.18×101 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
peptidylprolyl isomerase Kratky plot 1.104 0 √3 sRg
p(r)
peptidylprolyl isomerase pair distance distribution function Rg: 3.9 nm 0 Dmax: 12.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
peptidylprolyl isomerase DAMMIN model
Synchrotron SAXS data from solutions of chloroplast trigger factor from Chlamydomonas reinhardtii in 20 mM Tris pH 7.5, 150 mM KCl were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 8 mg/ml were measured at 20°C. 10 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 concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

peptidylprolyl isomerase (CrTIG1)
Mol. type   Protein
Organism   Chlamydomonas reinhardtii
Olig. state   Monomer
Mon. MW   53.7 kDa
 
UniProt   A8JD56 (68-548)
Sequence   FASTA