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

TitleCrystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus.
Publication TypeJournal Article
Year of Publication2011
AuthorsFislage, M., M. Roovers, S. Münnich, L. Droogmans, and W. Versées
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume67
IssuePt 11
Pagination1432-5
Date Published2011 Nov 1
ISSN1744-3091
KeywordsCrystallization, Crystallography, X-Ray, Pyrococcus furiosus, Thermus thermophilus, tRNA Methyltransferases
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.

DOI10.1107/S1744309111036347
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID22102250
PubMed Central IDPMC3212469