title: Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus.
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 Å 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 Å resolution.
authors.affiliation: VIB Department of Structural Biology, Pleinlaan 2, 1050 Brussels, Belgium. marcus.fislage@vib-vub.be
authors.forename: Marcus
authors.initials: M
authors.lastname: Fislage
authors.forename: Martine
authors.initials: M
authors.lastname: Roovers
authors.forename: Stefan
authors.initials: S
authors.lastname: Münnich
authors.forename: Louis
authors.initials: L
authors.lastname: Droogmans
authors.forename: Wim
authors.initials: W
authors.lastname: Versées
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D020027:Pyrococcus furiosus / Q000201:enzymology*; D016963:Thermus thermophilus / Q000201:enzymology*; D012359:tRNA Methyltransferases / Q000737:chemistry*
chemical_list: D012359:tRNA Methyltransferases
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