title: Crystallization and preliminary X-ray analysis of the archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii.
abstract: The archaeosine tRNA-guanine transglycosylase from the hyperthermophilic archaeon Pyrococcus horikoshii was crystallized and preliminary X-ray characterization was performed. Single crystals were grown by the hanging-drop vapour-diffusion method, using sodium/potassium phosphate and sodium acetate as precipitants. The space group is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 99.28 (14), c = 363.74 (56) A. The cryocooled crystals diffracted X-rays beyond 2.2 A resolution using synchrotron radiation from station BL44XU at SPring-8 (Harima). Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.
authors.affiliation: Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
authors.forename: R
authors.initials: R
authors.lastname: Ishitani
authors.forename: O
authors.initials: O
authors.lastname: Nureki
authors.forename: T
authors.initials: T
authors.lastname: Kijimoto
authors.forename: M
authors.initials: M
authors.lastname: Watanabe
authors.forename: H
authors.initials: H
authors.lastname: Kondo
authors.forename: N
authors.initials: N
authors.lastname: Nameki
authors.forename: N
authors.initials: N
authors.lastname: Okada
authors.forename: S
authors.initials: S
authors.lastname: Nishimura
authors.forename: S
authors.initials: S
authors.lastname: Yokoyama
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D010430:Pentosyltransferases / Q000737:chemistry*; D011487:Protein Conformation; D019711:Pyrococcus / Q000201:enzymology*; D012645:Selenomethionine / Q000737:chemistry
chemical_list: D012645:Selenomethionine; D010430:Pentosyltransferases; C020837:queuine tRNA-ribosyltransferase