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. 2008 Jun 27;190(17):5766–5780. doi: 10.1128/JB.01930-07

FIG. 3.

FIG. 3.

Fluorescence quenching of wild-type MacRPA1 and its chimeras. Reaction mixtures contain a fixed amount of wild-type (WT) MacRPA1 or its chimeras (1 μM). Increasing amounts of φ174 phage ssDNA were then added, and the fluorescence at 340 nm was measured at 20°C with an excitation wavelength of 280 nm. The percentage of free RPA was determined by the changes in fluorescence with MacRPA1 and its chimeras. The binding site sizes for wild-type MacRPA1, MacRPA1 chimera-1, MacRPA1 chimera-2 (MbuRPA1-like protein), MacRPA1 chimera-3, MjaRPA-like protein, and MthRPA-like protein were calculated to be 11.1 ± 0.8, 9.0 ± 0.6, 11.4 ± 0.9, 9.1 ± 1.2, 11.4 ± 0.6, and 9.2 ± 1.0 nucleotides (nt), respectively, per monomer.