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 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.
D001395:Azotobacter / Q000201:enzymology; D003013:Clostridium / Q000201:enzymology; D005288:Ferredoxins; D008983:Molybdoferredoxin; D009591:Nitrogenase; D011487:Protein Conformation; D014961:X-Ray Diffraction
D005288:Ferredoxins; D008983:Molybdoferredoxin; D009591:Nitrogenase