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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

Onderzoeksoutput: Articlepeer review

3 Citaten (Scopus)

Samenvatting

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.
Originele taal-2English
Pagina's (van-tot)1432-1435
Aantal pagina's4
TijdschriftActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
StatusPublished - 1 nov. 2011

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