Purification, crystallization and initial X-ray diffraction study of the zinc-finger domain of zebrafish Nanos

Abstract

Nanos is a highly conserved RNA-binding protein in higher eukaryotes and acts as a key regulator protein involved in translational control utilizing the 3′ untranslated region of mRNA. The C-terminal domain of Nanos has two conserved and novel CCHC-type zinc-finger motifs that are responsible for the function of Nanos. To clarify the structural basis of the function of Nanos, the C - terminal domain (residues 59-159) of zebrafish Nanos was overexpressed, purified and crystallized. The crystal belonged to space group P63, with unit-cell parameters a = b = 100.9, c = 71.5 Åγ= 120°. Structure determination by the MAD/SAD method is now in progress. © 2009 International Union of Crystallography All rights reserved.