Critical evaluation of a crystal structure of nitrogenase with bound N₂ ligands.

ABSTRACT: Recently, a 1.83 Å crystallographic structure of nitrogenase was suggested to show N₂-derived ligands at three sites in the catalytic FeMo cluster, replacing the three [Formula: see text] bridging sulfide ligands (two in one subunit and the third in the other subunit) (Kang et al. in Science 368: 1381-1385, 2020). Naturally, such a structure is sensational, having strong bearings on the reaction mechanism of the enzyme. Therefore, it is highly important to ensure that the interpretation of the structure is correct. Here, we use standard crystallographic refinement and quantum refinement to evaluate the structure. We show that the original crystallographic raw data are strongly anisotropic, with a much lower resolution in certain directions than others. This, together with the qu

SUBMITTER: Bergmann J 

PROVIDER: S-EPMC8068654 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature