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Literature summary for 7.1.2.2 extracted from

  • Maegawa, Y.; Morita, H.; Yao, M.; Watanabe, N.; Tanaka, I.
    Crystallization and preliminary X-ray diffraction study of the catalytic subunit of archaeal H+-transporting ATP synthase from Pyrococcus horikoshii OT3 (2004), Acta Crystallogr. Sect. D, 60, 1484-1486.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the catalytic subunit A of the archaeal-type H+-ATPase is cloned and expressed in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
the catalytic subunit A of the archaeal-type H+-ATPase is crystallized by hanging-drop vapour-diffusion method with 2-methyl-2,4-pentanediol as a precipitant. X-ray intensity data are collected to 2.55 A resolution. The crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 128.0, c = 104.7 A, and contain one molecule per asymmetric unit Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
subunit A, gel filtration Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57728 catalytic subunit A
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Pyrococcus horikoshii OT-3 O57728 catalytic subunit A
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
H+-ATPase
-
Pyrococcus horikoshii
H+-transporting ATP synthase
-
Pyrococcus horikoshii