Skip to main content
padlock icon - secure page this page is secure

Cloning, expression, purification, crystallization and preliminary crystallographic analysis of NifH2 from Methanocaldococcus jannaschii

Buy Article:

$52.00 + tax (Refund Policy)

Nitrogenases are protein complexes that are only found in Azotobacter and are required for biological nitrogen fixation. They are made up of a nitrogenase, which is a NifD2/NifK2 heterotetramer, and a nitrogenase reductase, which is a homodimer of NifH. Many homologues of nitrogenase have been found in various non‐nitrogen‐fixing prokaryotes; in particular, they are found in all known methanogens. This indicates that these homologues may play a role in methane production. Here, the cloning of NifH2, a homologue of the NifH nitrogenase component, from Methanocaldococcus jannaschii (MjNifH2) and its expression in Escherichia coli with a polyhistidine tag, purification and crystallization are described. MjNifH2 crystals were obtained by the hanging‐drop vapour‐diffusion method and diffracted to a resolution limit of 2.85 Å. The crystals belonged to space group P2, with unit‐cell parameters a = 64.01, b = 94.38, c = 98.08 Å, α = γ = 90, β = 98.85°.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Methanocaldococcus jannaschii; NifH2; nitrogen fixation; nitrogenases

Document Type: Research Article

Publication date: January 1, 2011

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more