Unfortunately, im not finding a great review of current SPA data processing bu the cryoSPARC case studies can give a good idea of where things are: guide.cryosparc.com/processing-d...

For a pretty good (although detailed) book: iopscience.iop.org/book/edit/97...

And pretty good review of sample prep and imaging: www.sciencedirect.com/science/arti...

The paper can be found here: www.nature.com/articles/s41...

7) This was an exciting study led by Sarah Narehood in collaboration with Suppachai Srisantitham, Vanessa Eng, Angela Shiau, Kelly McGuire, David Britt. #cryoEM #cryoSPARC #Nitrogenase #HerizkLab @nature.com @sptlabtech.bsky.social @structurabio.bsky.social #UCSDChemBioChem #anaerobicEM

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!

2) The only known nitrogen fixing enzyme employed by microbes is nitrogenase, a highly oxygen sensitive protein complex. In this study we were able to determine multiple structures of Nitrogenase in complex with the small protein Shethna (FeSII), solving a decades long mystery.