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. 2023 Dec 7;31(1):150–158. doi: 10.1038/s41594-023-01124-2

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — a, SDS–PAGE analysis of the purified Fe nitrogenase reductase component (AnfH) and catalytic component (AnfDGK). MM, molecular mass. b, In vitro activity assays of the purified Fe nitrogenase under Ar or N₂ atmosphere. Plotted are the specific activities for NH₃ (top) or H₂ (bottom) formation under varying molar ratios of AnfH₂ to Anf(DGK)₂. Individual measurements (n = 3) are shown, and the solid line represents the non-linear fit of the data. c, Mass photometry analysis of the individual nitrogenase components (top and middle) and the AlF₃-trapped Anf(DGK)₂(H₂)₂ complex (bottom). Plotted are the number of events versus the molecular mass of the individual events (in kDa). d, Electron density map of the AlF₃-trapped Fe nitrogenase complex at a global resolution of 2.35 Å (EMD-16890).

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