title: Crystallization and preliminary X-ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1.
abstract: Thioredoxin peroxidase is a member of the peroxiredoxin family and plays a dominant role in a hydrogen peroxide metabolism. A recombinant form of the hyperthermostable thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1, a polypeptide consisting of 250 amino acids, was purified. The C207S mutant protein was crystallized by the hanging-drop vapour-diffusion method using potassium sodium tartrate as the precipitant at 298 K. Diffraction data were collected and processed to 2.7 A resolution. The crystal belongs to space group P1, with unit-cell parameters a = 126.2, b = 126.3, c = 213.7 A, alpha = 80.4, beta = 80.3, gamma = 70.7 degrees. Calculation of the self-rotation function showed that the protein quaternary structure includes a fivefold axis and five twofold axes.
authors.affiliation: National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka 563-8577, Japan. nakamura-t@aist.go.jp
authors.forename: Tsutomu
authors.initials: T
authors.lastname: Nakamura
authors.forename: Hiroyoshi
authors.initials: H
authors.lastname: Matsumura
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Inoue
authors.forename: Yasushi
authors.initials: Y
authors.lastname: Kai
authors.forename: Koichi
authors.initials: K
authors.lastname: Uegaki
authors.forename: Yoshihisa
authors.initials: Y
authors.lastname: Hagihara
authors.forename: Mitsuo
authors.initials: M
authors.lastname: Ataka
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Ishikawa
mesh_terms: D041522:Aeropyrum / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology; D010544:Peroxidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D054464:Peroxiredoxins; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D010544:Peroxidases; D054464:Peroxiredoxins