Expression, purification and preliminary crystallographic studies of a single-point mutant of Mos1 mariner transposase

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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


Publication date: May 1, 2004



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