Crystallization of an intact GST-estrogen receptor hormone binding domain fusion protein

Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):423-6. doi: 10.1107/s0907444997011086.

Abstract

Crystals of an intact GST-estrogen receptor hormone binding domain fusion protein have been grown from solutions of MPD. The crystals grew as clusters of thin plates and needles of maximum dimensions 100 x 20 x 1 micrometer but were unsuitable for X-ray diffraction analysis. However, examination by electron microscopy shows an ordered lattice in which the protein molecules are clearly visible. Image analysis of electron micrographs of the protein crystals revealed electron stain-excluding density which showed a two-domain trimeric structure in projection, with each molecule of dimensions 12.0 x 5.0 nm diameter. The use of GST-fusion proteins in crystallisation are discussed.

MeSH terms

  • Crystallization
  • Glutathione Transferase / chemistry*
  • Ligands
  • Microscopy, Electron
  • Protein Structure, Tertiary*
  • Receptors, Estrogen / chemistry*
  • Recombinant Fusion Proteins / chemistry*

Substances

  • Ligands
  • Receptors, Estrogen
  • Recombinant Fusion Proteins
  • Glutathione Transferase