Cadmium-induced crystallization of proteins: II. Crystallization of the Salmonella typhimurium histidine-binding protein in complex with L-histidine, L-arginine, or L-lysine

Sergei Trakhanov, David I. Kreimer, Sean Parkin, Giovanna Ferro Luzzi Ames, Bernhard Rupp

Research output: Contribution to journalArticlepeer-review

40 Scopus citations

Abstract

To further investigate favorable effects of divalent cations on the formation of protein crystals, three complexes of Salmonella typhimurium histidine-binding protein were crystallized with varying concentrations of cadmium salts. For each of the three histidine-binding protein complexes, cadmium cations were found to promote or improve crystallization. The optimal cadmium concentration is ligand specific and falls within a narrow concentration range. In each case, crystals grown in the presence of cadmium diffract to better than 2.0 Å resolution and belong to the orthorhombic space group P212121. From our results and from the analysis of cadmium sites in well-refined protein structures, we propose that cadmium addition provides a generally useful technique to modify crystal morphology and to improve diffraction quality.

Original languageEnglish
Pages (from-to)600-604
Number of pages5
JournalProtein Science
Volume7
Issue number3
DOIs
StatePublished - Mar 1998

Keywords

  • Cadmium addition
  • Crystal growth
  • Crystal morphology
  • Crystallization
  • Histidine binding protein
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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