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Literature summary for 1.18.6.1 extracted from

  • Huang, K.; Ma, J.; Yuan, Y.; Gao, Y.
    Cloning, expression, purification, crystallization and preliminary crystallographic analysis of NifH2 from Methanocaldococcus jannaschii (2011), Acta Crystallogr. Sect. F, 67, 133-135.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene MJ0685, expression of His-tagged NifH2 in Escherichia coli strain BL21 (DE3) Methanocaldococcus jannaschii

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged NifH2, hanging drop vapour diffusion method, 0.001 l of 20 mg/ml protein in 2 mM Tris-HCl, pH 8.0, and 50 mM NaCl, is mixed with 0.001 ml of reservoir solution, containing 0.1 M sodium citrate, 8% PEG 8000, pH 5.0, and equilibrated against 0.15 ml of reservoir solution, 10 days, 4°C, X-ray diffraction structure determination and analysis at 2.85 A resolution Methanocaldococcus jannaschii

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
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NifH2 is one of two homologues of NifH in Methanocaldococcus jannaschii
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged NifH2 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration to over 95% purity Methanocaldococcus jannaschii

Synonyms

Synonyms Comment Organism
NifH2
-
Methanocaldococcus jannaschii

General Information

General Information Comment Organism
additional information nitrogenase is a protein complex that is required for biological nitrogen fixation. It is made up of a nitrogenase, which is a NifD2/NifK2 heterotetramer, and a nitrogenase reductase, which is a homodimer of NifH Methanocaldococcus jannaschii