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

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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°.
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Keywords: Methanocaldococcus jannaschii; NifH2; nitrogen fixation; nitrogenases

Document Type: Research Article

Publication date: January 1, 2011

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