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 Dec 12)
PMID: 30552875
doi: 10.1016/j.jmb.2018.12.005 		Submitted to SASBDB: 2018 Oct 29
Published in SASBDB:

SASDEZ6 – Gamma-crystallin S disulfide-linked dimer

Gamma-crystallin S experimental SAS data
DAMMIN model
Sample: Gamma-crystallin S dimer, 42 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
RgGuinier 2.4 nm
Dmax 7.5 nm
VolumePorod 45 nm3

SASDE27 – Gamma-crystallin S monomer

Gamma-crystallin S experimental SAS data
CHIMERA model
Sample: Gamma-crystallin S monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 27 nm3