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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 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 language | English |
|---|---|
| Pages (from-to) | 962-964 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 60 |
| Issue number | Pt 5 |
| DOIs | |
| Publication status | Published - May 2004 |
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Dive into the research topics of 'Expression, purification and preliminary crystallographic studies of a single-point mutant of Mos1 mariner transposase'. Together they form a unique fingerprint.Projects
- 1 Finished
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Targeted integration and the mechanism of transposition of a mariner transposable element
Finnegan, D. (Principal Investigator)
Biotechnology and Biological Sciences Research Council
1/09/04 → 31/10/07
Project: Research