Crystallization and preliminary X-ray crystallographic analysis of a ytfG gene product from Escherichia coli

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):365-7. doi: 10.1107/S0907444903027781. Epub 2004 Jan 23.

Abstract

The Escherichia coli ytfG gene product, with NAD(P)H:quinone oxidoreductase activity, was crystallized by the hanging-drop vapour-diffusion method at 296 K. A 1.78 A data set has been collected using synchrotron radiation at Pohang Light Source, South Korea. The crystal belongs to the primitive trigonal system, with unit-cell parameters a = b = 81.7, c = 76.8 A. Analysis of the packing density shows that the asymmetric unit probably contains one monomer, with a solvent content of 48.8%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray / methods*
  • Cytoplasm / metabolism
  • Escherichia coli / enzymology*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • NADH, NADPH Oxidoreductases / chemistry*
  • Oxidoreductases / chemistry
  • Polyethylene Glycols / chemistry
  • Polymerase Chain Reaction
  • Recombinant Proteins / chemistry
  • Solvents
  • Synchrotrons
  • Temperature

Substances

  • Escherichia coli Proteins
  • Recombinant Proteins
  • Solvents
  • Polyethylene Glycols
  • Oxidoreductases
  • NADH, NADPH Oxidoreductases
  • ytfG protein, E coli