Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii

Crystallographic properties of the MoFe proteins of nitrogenase from Clostridium pasteurianum and Azotobacter vinelandii

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 P21space group. The MoFe protein crystals from C. pasteurianum and A. vinelandii diffract to an...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1982-01, Vol.79 (2), p.378-380
Hauptverfasser: Weininger, M.S, Mortenson, L.E
Format: Artikel
Sprache:eng
Schlagworte:
Atoms
Azotobacter - enzymology
Azotobacter vinelandii
Biochemistry
Biological Sciences
Catalysis
Clostridium
Clostridium - enzymology
Clostridium pasteurianum
Crystals
Ferredoxins
Molecules
Molybdoferredoxin
Nitrogenase
Precession
Protein Conformation
Symmetry
X-Ray Diffraction
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Zusammenfassung: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 P21space group. The MoFe protein crystals from C. pasteurianum and A. vinelandii diffract to angles corresponding to resolutions as great as 2.4 angstrom and 3.0 angstrom, respectively. The cell dimensions of the MoFe protein crystals from the two species have been determined from precession photographs.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.2.378