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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 Angstrom resolution and show tetragonal symmetry, with unit-cell parameters a = b = 44.5, c = 205.6 Angstrom. Multiple-wavelength anomalous data from a selenomethionyl form of the protein and data from a heavy-atom derivative have been collected.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Issue number||Pt 5|
|Publication status||Published - May 2004|
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