Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus

Marcus Fislage, M. Roovers, Stefan Münnich, L. Droogmans, Wim Versees

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

Abstract

Methyltransferases form a major class of tRNA-modifying enzymes that are needed for the proper functioning of tRNA. Here, the expression, purification and crystallization of two related putative tRNA methyltransferases from two kingdoms of life are reported. The protein encoded by the gene pf1002 from the archaeon Pyrococcus furiosus was crystallized in the monoclinic space group P2(1). A complete data set was collected to 2.2 angstrom resolution. The protein encoded by the gene ttc1157 from the eubacterium Thermus thermophilus was crystallized in the trigonal space group P3(2)21. A complete data set was collected to 2.05 angstrom resolution.
Original languageEnglish
Pages (from-to)1432-1435
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Publication statusPublished - 1 Nov 2011

Keywords

  • tRNA modification
  • crystallization

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