Crystallization and preliminary X-ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Tsutomu NakamuraKazuhiko Ishikawa

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.

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Citations

Apr 26, 2008·Proceedings of the National Academy of Sciences of the United States of America·Tsutomu NakamuraTsuyoshi Inoue
Jul 9, 2013·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Tsutomu NakamuraTsuyoshi Inoue
Dec 19, 2020·Bioconjugate Chemistry·Tomoki HimiyamaTsutomu Nakamura

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