6) We were able to achieve these structures using our newly developed (an)aerobic freezing protocol using the SPT chameleon. This allowed us to generate high quality girds with thin ice without having to be in an anaerobic chamber!
www.biorxiv.org/content/10.1...

5) Our structures combined with our analytical ultracentrifugation and EPR experiments allow us to propose a mechanism by which these oxygen protecting complexes and filaments form in oxidizing conditions, protecting MoFeP and FeP, and disassemble in reducing conditions.

4) Surprisingly, the binding of Shethna occurs at the catalytic interface of both MoFeP and FeP! Preventing nitrogen fixation while also protecting the oxygen sensitive metal clusters harbored by both MoFeP and FeP.

3) We show that Shetna is capable of binding both the catalytic (MoFeP) and reductant (FeP) subunits, creating oxygen protecting complex. Fascinatingly, this complex is capable of forming higher order complexes and ultimately filaments!

1) Since I am the only Herzik lab member on @bsky.app, I get the privilege to announce our most recent publication from the Herzik/Tezcan labs. I got the wonderful opportunity to contribute on the cryoEM study of the oxygen protection mechansim employed by cells to protect Nitrogenase!