Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jul 1;62(Pt 7):662-4. doi: 10.1107/S1744309106020136. Epub 2006 Jun 10.

Abstract

Ferredoxin-NADP+ reductase (FNR) is an FAD-containing enzyme that catalyzes electron transfer between NADP(H) and ferredoxin. Here, results are reported of the recombinant expression, purification and crystallization of FNR from Leptospira interrogans, a parasitic bacterium of animals and humans. The L. interrogans FNR crystals belong to a primitive monoclinic space group and diffract to 2.4 angstroms resolution at a synchrotron source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Electron Transport
  • Ferredoxin-NADP Reductase / chemistry*
  • Ferredoxin-NADP Reductase / isolation & purification*
  • Ferredoxins / metabolism
  • Flavin-Adenine Dinucleotide / metabolism
  • Leptospira interrogans / enzymology*
  • NADP / metabolism
  • Protein Conformation
  • X-Ray Diffraction

Substances

  • Ferredoxins
  • Flavin-Adenine Dinucleotide
  • NADP
  • Ferredoxin-NADP Reductase