Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human γS-crystallin

gamma S-crystallin is a major structural component of the human eye lens, which maintains its stability over the lifetime of an organism with negligible turnover. The G57W mutant of human gamma S-crystallin (abbreviated hereafter as gamma S-G57W) is associated with dominant congenital cataracts. In order to provide a structural basis for the ability of gamma S-G57W causing cataract, we have cloned, overexpressed, isolated and purified the protein. The 2D [N-15-H-1]-HSQC spectrum recorded with uniformly C-13/N-15-labelled gamma S-G57W was highly dispersed indicating the protein to adopt an ordered conformation. In this paper, we report almost complete sequence-specific H-1, C-13 and N-15 resonance assignments of gamma S-G57W using a suite of heteronuclear 3D NMR experiments.