Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV from Thermotoga maritima

Ronny C. Hughes, Stephen J. Tomanicek, Joseph D. Ng, Leighton Coates

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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.

Original languageEnglish
Pages (from-to)1317-1319
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number12
DOIs
StatePublished - 2009

Keywords

  • DNA-repair proteins
  • Endonuclease IV
  • Thermotoga maritima

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