Crystallization and preliminary X-ray diffraction analysis of the homing endonuclease I-CvuI from Chlorella vulgaris in complex with its target DNA

Acta Crystallogr F Struct Biol Commun. 2014 Feb;70(Pt 2):256-9. doi: 10.1107/S2053230X1400065X. Epub 2014 Jan 22.

Abstract

Homing endonucleases are highly specific DNA-cleaving enzymes that recognize long stretches of DNA. The engineering of these enzymes provides novel instruments for genome modification in a wide range of fields, including gene targeting, by inducing specific double-strand breaks. I-CvuI is a homing endonuclease from the green alga Chlorella vulgaris. This enzyme was purified after overexpression in Escherichia coli. Crystallization experiments of I-CvuI in complex with its DNA target in the presence of Mg(2+) yielded crystals suitable for X-ray diffraction analysis. The crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 62.83, b = 83.56, c = 94.40 Å. The self-rotation function and the Matthews coefficient suggested the presence of one protein-DNA complex per asymmetric unit. The crystals diffracted to a resolution limit of 1.9 Å using synchrotron radiation.

Keywords: Chlorella vulgaris; gene targeting; homing endonuclease I-CvuI; protein–DNA interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlorella vulgaris / enzymology*
  • Chromatography, Liquid
  • Crystallization
  • Crystallography, X-Ray / methods*
  • DNA / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Endonucleases / chemistry*
  • Endonucleases / metabolism
  • Protein Conformation

Substances

  • DNA
  • Endonucleases