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

Authors
  • de Ruyck, Jerome
  • Schubert, Heidi L
  • Janczak, Matthew W
  • Poulter, C Dale
Type
Published Article
Journal
Acta crystallographica. Section F, Structural biology communications
Publication Date
Mar 01, 2014
Volume
70
Issue
Pt 3
Pages
347–349
Identifiers
DOI: 10.1107/S2053230X14002143
PMID: 24598924
Source
Medline
Keywords
License
Unknown

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.

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