title: Crystallization and preliminary X-ray diffraction analysis of ribosomal protein L11 methyltransferase from Thermus thermophilus HB8.
abstract: Ribosomal proteins are subjected to a variety of post-translational modifications, of which methylation is the most frequently found in all three kingdoms of life. PrmA is the only bacterial enzyme identified to date that catalyzes the methylation of a ribosomal protein. It is responsible for the introduction of nine methyl groups into the N-terminal domain of ribosomal protein L11. The PrmA protein from Thermus thermophilus HB8 was crystallized and a preliminary X-ray diffraction analysis was performed. A cryocooled crystal diffracted X-rays beyond 1.9 A using synchrotron radiation.
authors.affiliation: RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Kaminishi
authors.forename: Hiroaki
authors.initials: H
authors.lastname: Sakai
authors.forename: Chie
authors.initials: C
authors.lastname: Takemoto-Hori
authors.forename: Takaho
authors.initials: T
authors.lastname: Terada
authors.forename: Noriko
authors.initials: N
authors.lastname: Nakagawa
authors.forename: Nobuko
authors.initials: N
authors.lastname: Maoka
authors.forename: Seiki
authors.initials: S
authors.lastname: Kuramitsu
authors.forename: Mikako
authors.initials: M
authors.lastname: Shirouzu
authors.forename: Shigeyuki
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism*; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C027624:ribosomal protein L11; C084165:L11 methyltransferase; D008780:Methyltransferases