The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation.

Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA, J Mol Biol (2018) Europe PMC

SASDEZ6 – Gamma-crystallin S disulfide-linked dimer

Gamma-crystallin S
MWI(0) 36 kDa
MWexpected 42 kDa
VPorod 45 nm3
log I(s) 5.49×102 5.49×101 5.49×100 5.49×10-1
Gamma-crystallin S small angle scattering data  s, nm-1
ln I(s)
Gamma-crystallin S Guinier plot ln 5.49×102 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Gamma-crystallin S Kratky plot 1.104 0 √3 sRg
p(r)
Gamma-crystallin S pair distance distribution function Rg: 2.4 nm 0 Dmax: 7.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Gamma-crystallin S DAMMIN model
log I(s)
 s, nm-1
Gamma-crystallin S CHIMERA model
SAXS data from solutions of gamma-crystallin S, disulfide-linked dimer, in 20 mM sodium phosphate, pH 7 were collected on the Bruker Nanostar II instrument at the Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering (ANSTO/ACNS, Sydney, Australia) using a multiwire Bruker Hi-Star detector at a sample-detector distance of 0.7 m and at a wavelength of λ = 0.1541 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.00 mg/ml was measured at 25°C. Four successive 3600 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.

Gamma-crystallin S
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   21.0 kDa
 
UniProt   P22914
Sequence   FASTA
 
PDB ID   6FD8