Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy.

Xu X, Reinle W, Hannemann F, Konarev PV, Svergun DI, Bernhardt R, Ubbink M, J Am Chem Soc 130(20):6395-403 (2008) Europe PMC

SASDAP5 – Native complex CytC_Adr

Cytochrome C dimer
Adrenodoxin dimer
MWI(0) 42 kDa
MWexpected 44 kDa
VPorod 64 nm3
log I(s) 1.13×101 1.13×100 1.13×10-1 1.13×10-2
Cytochrome C dimer Adrenodoxin dimer small angle scattering data  s, nm-1
ln I(s)
Cytochrome C dimer Adrenodoxin dimer Guinier plot ln 1.13×101 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Cytochrome C dimer Adrenodoxin dimer Kratky plot 1.104 0 3 sRg
p(r)
Cytochrome C dimer Adrenodoxin dimer pair distance distribution function Rg: 3 nm 0 Dmax: 9.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Cytochrome C dimer Adrenodoxin dimer DAMMIN model

log I(s)
 s, nm-1
Cytochrome C dimer Adrenodoxin dimer SASREF model

Synchrotron SAXS data from solutions of Native complex CytC_Adr in 20 mM HEPES 2 mM DTT, pH 7.4 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.4 and 24 mg/ml were measured at 15°C. Two successive 120 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.

Tags: X33
Cytochrome C dimer (Cyt_C_dimer)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   11 kDa
Sequence   FASTA
 
Adrenodoxin dimer (Adrenodoxin dimer)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Dimer
Mon. MW   11 kDa
Sequence   FASTA