Crystallization and 7 A resolution electron density map of the large fragment of Escherichia coli DNA polymerase I

J Mol Biol. 1983 May 25;166(3):453-6. doi: 10.1016/s0022-2836(83)80095-3.

Abstract

Crystals of the large fragment of Escherichia coli DNA polymerase I have been grown that diffract to better than 2.8 A resolution. They are in tetragonal space group P4(3) with a = b = 104.1 A, c = 86 A. A 7 A resolution map shows the protein to consist of two domains and to be mostly alpha-helical. The active site has been located by binding nucleoside monophosphates.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Crystallization
  • Crystallography
  • DNA Polymerase I*
  • DNA-Directed DNA Polymerase*
  • Escherichia coli / enzymology*
  • Nucleotides

Substances

  • Nucleotides
  • DNA Polymerase I
  • DNA-Directed DNA Polymerase