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Literature summary for 1.11.1.24 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
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Aeropyrum pernix

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9Y9L0
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-
Aeropyrum pernix DSM 11879 Q9Y9L0
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-

Purification (Commentary)

Purification (Comment) Organism
-
 Aeropyrum pernix