Open AccessCrystallization and preliminary X‐ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1
Author(s) -
Nakamura Tsutomu,
Matsumura Hiroyoshi,
Inoue Tsuyoshi,
Kai Yasushi,
Uegaki Koichi,
Hagihara Yoshihisa,
Ataka Mitsuo,
Ishikawa Kazuhiko
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105005294
Subject(s) - crystallography , chemistry , peroxiredoxin , peroxidase , orthorhombic crystal system , crystallization , thioredoxin , crystal structure , biochemistry , enzyme , organic chemistry
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 Å resolution. The crystal belongs to space group P 1, with unit‐cell parameters a = 126.2, b = 126.3, c = 213.7 Å, α = 80.4, β = 80.3, γ = 70.7°. Calculation of the self‐rotation function showed that the protein quaternary structure includes a fivefold axis and five twofold axes.