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Article

Improved crystallization of Escherichia coli ATP synthase catalytic complex (F1) by introducing a phosphomimetic mutation in subunit ε.

Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Oct 2012

Roy Ankoor, Hutcheon Marcus L, Duncan Thomas M, Cingolani Gino

Abstract excerpt

The bacterial ATP synthase (F(O)F(1)) of Escherichia coli has been the prominent model system for genetics, biochemical and more recently single-molecule studies on F-type ATP synthases. With 22 total polypeptide chains (total mass of ∼529 kDa), E. coli F(O)F(1) represents nature's smallest rotary motor, composed of a membrane-embedded proton transporter (F(O)) and a peripheral catalytic complex (F(1)). The...

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Identifiers

PMID: 23027754
DOI: 10.1107/S1744309112036718
PMCID: PMC3490465

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Source receipt: pubmed, retrieved 7 Sept 2026.

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