Tetartohedral twinning in IDI-2 from Thermus thermophilus: crystallization under anaerobic conditions

Jérôme De Ruyck, Heidi L. Schubert, Matthew W. Janczak, C. Dale Poulter

Research output: Contribution to journalArticlepeer-review

Abstract

Type-2 isopentenyl diphosphate isomerase (IDI-2) is a key flavoprotein involved in the biosynthesis of isoprenoids. Since fully reduced flavin mononucleotide (FMNH2) is needed for activity, it was decided to crystallize the enzyme under anaerobic conditions in order to understand how this reduced cofactor binds within the active site and interacts with the substrate isopentenyl diphosphate (IPP). In this study, the protein was expressed and purified under aerobic conditions and then reduced and crystallized under anaerobic conditions. Crystals grown by the sitting-drop vapour-diffusion method and then soaked with IPP diffracted to 2.1 Å resolution and belonged to the hexagonal space group P6322, with unit-cell parameters a = b = 133.3, c = 172.9 Å. © 2014 International Union of Crystallography.

Original languageEnglish
Pages (from-to)347-9
Number of pages3
JournalActa Crystallographica. Section F: Structural Biology Communications
Volume70
Issue number3
DOIs
Publication statusPublished - 2014

Keywords

  • anaerobic
  • flavoprotein
  • IDI-2
  • isopentenyl diphosphate isomerase
  • isoprenoid
  • twinning

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