Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering

Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T, Biomolecules 12(1):95 (2022) DOI

SASDN62 – SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 6.4

Cytochrome c'
MWI(0) 27 kDa
MWexpected 27 kDa
VPorod 11 nm3
log I(s) 1.62×10-1 1.62×10-2 1.62×10-3 1.62×10-4
Cytochrome c' small angle scattering data  s, nm-1
ln I(s)
Cytochrome c' Guinier plot ln 1.63×10-1 Rg: 1.8 nm 0 (1.8 nm)-2 s2
Cytochrome c' Kratky plot 1.104 0 3 sRg
Cytochrome c' pair distance distribution function Rg: 1.8 nm 0 Dmax: 5.5 nm

Data validation

There are no models related to this curve.

SANS data from cytochrome c' in phosphate buffer, pD 6.4, were collected using the KWS1 SANS instrument (FRM2, Munich, Germany) equipped with a 6Li-Scintillator 1 mm thickness + photomultiplier detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.5 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.50 mg/ml was measured at 25°C. One 1800 second frame was 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.

Concentration min = UNKNOWN

Cytochrome c' (Cyt c')
Mol. type   Protein
Organism   Alcaligenes
Olig. state   Dimer
Mon. MW   13.6 kDa
UniProt   P00138 (1-127)
Sequence   FASTA