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. 2009 Dec 4;38(4):e25. doi: 10.1093/nar/gkp1089

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© The Author(s) 2009. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Improved attH × attPH recombination efficiency of integrase mutants translated in vitro. (A) The recombination efficiency of 74 integrase selectants on attP × attPH substrates was assayed using real-time PCR (Supplementary Figure S1) and results for the six best clones are shown. All activities are presented relative to activity of parental Int-h/218 with the attB × attP substrates (100%). Error bars indicate standard deviation of two independent experiments. (B) The efficiency of the six best selectants was also investigated for recombination between the non-cognate attH × attP substrate pair. (C) Recombination efficiency of the six selectants using attH × attPH substrates in the presence of 50-fold excess attB and attP competitors. Recombination of the competing attB. and attP substrates within the same reaction mix was also measured. Activities are presented relative to activity of parental Int-h/218 with the attP × attPH and attB × attP substrates (100%). (D) Recombination of endogenous attH site (attHgen) in genomic DNA by integrase selectants and Int-h/218. Activities are presented relative to activity of parental Int-h/218 (100%).