Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii.
AUTOR(ES)
Weininger, M S
RESUMO
Preliminary x-ray diffraction data from single crystals of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii have been obtained. Both protein crystals belong to the P2(1) space group. The MoFe protein crystals from C. pasteurianum and A. vinelandii diffract to angles corresponding to resolutions as great as 2.4 A and 3.0 A, respectively. The cell dimensions of the MoFe protein crystals from the two species have been determined from precession photographs.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=345741Documentos Relacionados
- Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii
- H2-uptake activity of the MoFe protein component of Azotobacter vinelandii nitrogenase.
- Nucleotide and deduced amino acid sequences of nifD encoding the alpha-subunit of nitrogenase MoFe protein of Clostridium pasteurianum.
- The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum.
- Electron Paramagnetic Resonance of Nitrogenase and Nitrogenase Components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP