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Crystallization and preliminary crystallographic studies of a bifunctional restriction endonuclease Eco57I

Authors
Publisher
Elsevier B.V.
Publication Date
Volume
1698
Issue
2
Identifiers
DOI: 10.1016/j.bbapap.2003.12.006
Keywords
  • Eco57I
  • Sinefungin
  • Restriction Endonuclease
  • Methyltransferase
Disciplines
  • Biology

Abstract

Abstract Restriction endonuclease Eco57I from Escherichia coli recognizes asymmetric DNA sequence 5′-CTGAAG and has both restriction (DNA cleavage a short distance away from the recognition site) and modification (methylation) activities residing in a single polypeptide chain. Single crystals of wild-type Eco57I ternary complexes with double-stranded DNA and sinefungin, a stimulator of endonuclease activity, were obtained by the vapor diffusion technique and characterized crystallographically for different variants of the DNA component. The best data for the complex with 25-mer DNA were collected to 4.2-Å resolution at 100 K using synchrotron radiation. The crystals are orthorhombic, space group P2 12 12, with a=164.3, b=293.0, c=71.1 Å, and contain two to four copies of the protein in the asymmetric unit.

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