Expression, purification and preliminary crystallographic studies of a single-point mutant of Mos1 mariner transposase
Authors: Richardson, Julia M.; Zhang, Lei; Marcos, Severine; Finnegan, David J.; Harding, Marjorie M.; Taylor, Paul; Walkinshaw, Malcolm D.
Source: Acta Crystallographica Section D, Volume 60, Number 5, May 2004 , pp. 962-964(3)
Abstract:A soluble single-point mutant of full-length Mos1 mariner transposase (MW = 40.7 kDa) has been overexpressed in Escherichia coli, purified to 95% homogeneity and crystallized. This provides the first example of the crystallization of a eukaryotic transposase. The native crystals diffract to 2.5 Å resolution and show tetragonal symmetry, with unit-cell parameters a = b = 44.5, c = 205.6 Å. Multiple-wavelength anomalous data from a selenomethionyl form of the protein and data from a heavy-atom derivative have been collected.
Document Type: Research Article
Publication date: May 1, 2004