Abstract
A restriction endonuclease, BstPI, was purified from a strain of B. stearothermophilus, and its cleavage specificity was determined. The enzyme cleaves at palindromic sites of the general structure: (Formula: see text) where N.N' can be any base pair. It produces phosphorylated 5'-termini which are single stranded over a length of 5 nucleotides. Ends generated by cleavage with BstPI can be rejoined by DNA ligase.
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