title: Stoichiometry of the α-complementation reaction of Escherichia coli β-galactosidase as revealed through single-molecule studies.
abstract: The α-complementation reaction of β-galactosidase was studied at single-molecule resolution using arrays of femtoliter-sized wells. Single molecules of the complementation species were observed to be stable for long periods of time, demonstrating that the α-complementation reaction is irreversible. By directly counting the number of active molecules formed in the complementation reaction when different concentrations of enzyme acceptor (EA) and enzyme donor (ED) are used, we deduce that the EA:ED ratio in the complementation species is 4:1.
authors: Department of Chemistry, Tufts University , 62 Talbot Avenue, Medford, Massachusetts 02155, United States.
authors: Pratyusha
authors: P
authors: Mogalisetti
authors: David R
authors: DR
authors: Walt
mesh_terms: D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry*; D001616:beta-Galactosidase / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D001616:beta-Galactosidase