title: Crystallization and preliminary X-ray crystallographic studies of phosphoglycerate kinase from Thermus caldophilus.
abstract: We report the purification and crystallization of phosphoglycerate kinase from Thermus caldophilus (Tca). The enzyme crystallizes in the P2(1)2(1)2(1) space group (cell dimensions a = 65.1, b = 71.3, c = 80.2 A), with one molecule in the asymmetric unit. A complete set of diffraction data was collected from an orthorhombic crystal up to 1.8 A resolution.
authors.affiliation: Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.
authors.forename: Jun Hyuck
authors.initials: JH
authors.lastname: Lee
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: Im
authors.forename: Seong-Hwan
authors.initials: SH
authors.lastname: Rho
authors.forename: Seong Ho
authors.initials: SH
authors.lastname: Park
authors.forename: Gil Bu
authors.initials: GB
authors.lastname: Kang
authors.forename: Su Jin
authors.initials: SJ
authors.lastname: Cho
authors.forename: Tae-Yeon
authors.initials: TY
authors.lastname: Kim
authors.forename: Hyun-Jae
authors.initials: HJ
authors.lastname: Shin
authors.forename: Dae-Sil
authors.initials: DS
authors.lastname: Lee
authors.forename: Soo Hyun
authors.initials: SH
authors.lastname: Eom
mesh_terms: D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000302:isolation & purification; D013824:Thermus / Q000201:enzymology*
chemical_list: D010735:Phosphoglycerate Kinase