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 A resolution and show tetragonal symmetry, with unit-cell parameters a = b = 44.5, c = 205.6 A. Multiple-wavelength anomalous data from a selenomethionyl form of the protein and data from a heavy-atom derivative have been collected.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray
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Drosophila Proteins / chemistry*
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Drosophila Proteins / genetics*
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Drosophila Proteins / isolation & purification
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Escherichia coli / genetics
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Molecular Sequence Data
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Point Mutation
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Protein Conformation
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Selenomethionine
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Transposases / chemistry*
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Transposases / genetics*
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Transposases / isolation & purification
Substances
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Drosophila Proteins
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Recombinant Proteins
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Selenomethionine
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Transposases