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)

Publisher: Blackwell Publishing

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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.

Keywords: Mos1 transposase; eukaryotic transposition; mariner/Tc1 transposons

Document Type: Research article

DOI: 10.1107/S0907444904003798

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