N2-bound Nitrogenase MoFe-protein from Azotobacter vinelandii

iron-sulfur-molybdenum cluster with interstitial carbon

Structural evidence for a dynamic metallocofactor during N2reduction by Mo-nitrogenase.

Flat Si Rh coated M0, Kirkpatrick-Baez flat bent Si M1 & M2

Liquid nitrogen-cooled double crystal Si(111)

Nitrogenase molybdenum-iron protein alpha chain

Nitrogenase molybdenum-iron protein beta chain

14-19 % w/v PEG smear high, 0.16M ammonium acetate, 0.1M sodium citrate (pH 5.0), 25.6 % v/v glycerol, 5mM Eu(II)-EGTA

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

Department of Energy (DOE, United States)

6VXT contains the same protein complex except for the ligands.

Authors state that the electron density of metal clusters presented in validation report and wwPDB websites are calculated from general pipeline without applying specific geometry restraints of the clusters. To reproduce accurate difference electron density map for the clusters, users should take the author-provided map coefficients presented in the structure factor file of the entry.

Nitrogenase molybdenum-iron protein alpha chain (E.C.1.18.6.1), Nitrogenase molybdenum-iron protein beta chain (E.C.1.18.6.1)

Azotobacter vinelandii, MoFe-protein, Fe-protein, FeMo-cofactor, oxidized P-cluster, OXIDOREDUCTASE