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Literature summary extracted from

  • Nakamura, T.; Matsumura, H.; Inoue, T.; Kai, Y.; Uegaki, K.; Hagihara, Y.; Ataka, M.; Ishikawa, K.
    Crystallization and preliminary X-ray diffraction analysis of thioredoxin peroxidase from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1 (2005), Acta Crystallogr. Sect. F, 61, 323-325.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 expression in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.24 the C207S mutant protein is 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° Aeropyrum pernix

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.24 C207S the C207S mutant protein is crystallized by the hanging-drop vapour-diffusion method Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Aeropyrum pernix Q9Y9L0
-
-
1.11.1.24 Aeropyrum pernix DSM 11879 Q9Y9L0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24
-
 Aeropyrum pernix