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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2009
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309109047393
- pmid
- 20054139
- Publisher site
- See Article on Publisher Site
Abstract
The DNA‐repair enzyme endonuclease IV from the thermophilic bacterium Thermotoga maritima MSB8 (reference sequence NC_000853) has been expressed in Escherichia coli and crystallized for X‐ray analysis. T. maritima endonuclease IV is a 287‐amino‐acid protein with 32% sequence identity to E. coli endonuclease IV. The protein was purified to homogeneity and was crystallized using the sitting‐drop vapor‐diffusion method. The protein crystallized in space group P61, with one biological molecule in the asymmetric unit, corresponding to a Matthews coefficient of 2.39 Å3 Da−1 and 47% solvent content. The unit‐cell parameters of the crystals were a = b = 123.2, c = 35.6 Å. Microseeding and further optimization yielded crystals with an X‐ray diffraction limit of 2.36 Å. A single 70° data set was collected and processed, resulting in an overall Rmerge and a completeness of 9.5% and 99.3%, respectively.
Journal
Acta Crystallographica Section F – Wiley
Published: Dec 1, 2009