Cryo-electron microscopy of a nitrogenase supercomplex from a methane-producing archaeon reveals a mechanism in which PII proteins drive assembly of such structures to regulate nitrogenase activity in response to nitrogen availability.
Cryo-electron microscopy of a nitrogenase supercomplex from a methane-producing archaeon reveals a mechanism in which PII proteins drive assembly of such structures to regulate nitrogenase activity in response to nitrogen availability.
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