Crystallization of a flavodoxin involved in nitrogen fixation in Rhodobacter capsulatus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):375-7. doi: 10.1107/S1744309108008038. Epub 2008 Apr 5.

Abstract

Flavodoxins are small electron-transfer proteins that contain one molecule of noncovalently bound flavin mononucleotide (FMN). The flavodoxin NifF from the photosynthetic bacterium Rhodobacter capsulatus is reduced by one electron from ferredoxin/flavodoxin:NADP(H) reductase and was postulated to be an electron donor to nitrogenase in vivo. NifF was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of PEG 3350 and PEG 400 at pH 5.5 and belong to the tetragonal space group P4(1)2(1)2, with unit-cell parameters a = b = 66.49, c = 121.32 A. X-ray data sets have been collected to 2.17 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Ferredoxin-NADP Reductase / metabolism
  • Flavodoxin / chemistry*
  • Flavodoxin / isolation & purification
  • Flavodoxin / metabolism
  • Nitrogen Fixation*
  • Rhodobacter capsulatus / enzymology*

Substances

  • Flavodoxin
  • Ferredoxin-NADP Reductase