Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of mouse dok1 protein

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):334-6. doi: 10.1107/S0907444903026696. Epub 2004 Jan 23.

Abstract

The PTB domain of mouse dok1 fusion protein has been overexpressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals have been obtained using the vapour-diffusion method and belong to space group P2(1)2(1)2(1). X-ray diffraction data were collected in-house to 2.5 A resolution. A selenomethionine (SeMet) dok1 PTB fusion-protein derivative was expressed using the same expression system, purified in a reductive environment and crystals were obtained under similar conditions. Subsequently, three different wavelength data sets from the derivative crystal were collected to 2.5 A resolution at SPring-8.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallography, X-Ray / methods*
  • DNA-Binding Proteins / chemistry*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / metabolism
  • Mice
  • Models, Molecular
  • Phosphoproteins / chemistry*
  • Polymerase Chain Reaction
  • Protein Structure, Tertiary
  • RNA-Binding Proteins / chemistry*
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Proteins / chemistry*

Substances

  • DNA-Binding Proteins
  • Dok1 protein, mouse
  • GAP-associated protein p62
  • Phosphoproteins
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Recombinant Proteins