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

J M Richardson, Lei Zhang, S Marcos, D J Finnegan, M M Harding, P Taylor, M D Walkinshaw

Research output: Contribution to journalArticlepeer-review

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 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.

Original languageEnglish
Pages (from-to)962-964
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue numberPt 5
DOIs
Publication statusPublished - May 2004

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