title: Expression, purification, crystallization and preliminary X-ray diffraction analysis of a galactose 1-phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum.
abstract: A galactose 1-phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum was crystallized using the sitting-drop vapour-diffusion method with polyethylene glycol 8000 as the precipitant. The crystals belonged to the tetragonal space group P4(1), with unit-cell parameters a = b = 73.3, c = 126.1 Å, and diffracted to 2.73 Å resolution on beamline BL5A at the Photon Factory. The overall R(merge) was 7.3% and the data completeness was 99.8%.
authors.affiliation: Department of Applied Chemistry and Biotechnology, Graduate School of Engineering, University of Fukui, 3-9-1 Bunkyo, Fukui 910-8507, Japan.
authors.forename: Takenori
authors.initials: T
authors.lastname: Satomura
authors.forename: Akihiro
authors.initials: A
authors.lastname: Hiraki
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Kawai
authors.forename: Ryushi
authors.initials: R
authors.lastname: Kawakami
authors.forename: Toshihisa
authors.initials: T
authors.lastname: Ohshima
authors.forename: Haruhiko
authors.initials: H
authors.lastname: Sakuraba
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression; D041543:Pyrobaculum / Q000201:enzymology*; D005694:UTP-Hexose-1-Phosphate Uridylyltransferase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D005694:UTP-Hexose-1-Phosphate Uridylyltransferase