Crystallization and preliminary X-ray crystallographic analysis of yeast NAD+-specific isocitrate dehydrogenase

Gang Hu, Alexander B. Taylor, Lee McAlister-Henn, P. John Hart

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


NAD+-specific isocitrate dehydrogenase (IDH; EC is a complex allosterically regulated enzyme in the tricarboxylic acid cycle. Yeast IDH is believed to be an octamer containing four catalytic IDH2 and four regulatory IDH1 subunits. Crystals of yeast IDH have been obtained and optimized using sodium citrate, a competitive inhibitor of the enzyme, as the precipitating agent. The crystals belong to space group R3, with unit-cell parameters a = 302.0, c = 112.1 Å. Diffraction data were collected to 2.9 Å from a native crystal and to 4.0 Å using multiwavelength anomalous diffraction (MAD) methods from an osmium derivative. Initial electron-density maps reveal large solvent channels and the molecular boundaries of the allosteric IDH multimer.

Original languageEnglish (US)
Pages (from-to)486-488
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number5
StatePublished - 2005

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics


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