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

SASDE27 – Gamma-crystallin S monomer

Gamma-crystallin S
MWI(0) 16 kDa
MWexpected 21 kDa
VPorod 27 nm3
log I(s) 1.31×102 1.31×101 1.31×100 1.31×10-1
Gamma-crystallin S small angle scattering data  s, nm-1
ln I(s)
Gamma-crystallin S Guinier plot ln 1.32×102 Rg: 1.8 nm 0 (1.8 nm)-2 s2
Gamma-crystallin S Kratky plot 1.104 0 3 sRg
Gamma-crystallin S pair distance distribution function Rg: 1.9 nm 0 Dmax: 5.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Gamma-crystallin S CHIMERA model

SAXS data from solutions of gamma-crystallin S monomer 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 3.00 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   Monomer
Mon. MW   21.0 kDa
UniProt   P22914
Sequence   FASTA
PDB code   2M3T