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5/5: Combining datasets collected with different LEA proteins computationally produced more isotropic reconstructions. Surprisingly, premixing multiple LEA proteins before grid preparation did not simply combine their effects and produced unexpected orientation distributions.

4/5: We've also explanded from two to six LEA proteins. All six protected Polα-primase from AWI damage but each produced a unique orientation distribution suggesting that AWI protection is a shared property while orientation control is LEA-specific.

3/5: HA trimer is a benchmark for severe preferred orientation. Adding LEA proteins dramatically broadened angular distribution coverage and improved map quality without relying on a stage-tilted data collection.

2/5: We've previously shown that LEA proteins AavLEA1 and RvLEAMshort can protect fragile samples from AWI damage, but we've found that these proteins can also alter sample orientation distributions.

1/5: Our latest preprint is out! We show that LEA proteins can diversify particle orientations in cryo-EM, helping to overcome preferred orientation at the air-water interface (AWI). www.biorxiv.org/cgi/content/... with @cijilim.bsky.social and Tim Grant #CryoEM #LEAproteins

It is so exciting to see our LEA proteins playing a role in solving this insane structure. Amazing work to the authors!

Our paper in Science is out! @souravagrawal.bsky.social, @rlynn.bsky.social, @susvirkar.bsky.social, and the rest of the team show human RPA is a telomerase processivity factor essential for telomere maintenance. This reshapes our thinking about telomerase regulation. www.science.org/doi/10.1126/...

Our new preprint revealing a new mechanism of mitochondrial disease pathophysiology: the accumulation of toxic complex I intermediates bound to complex III www.biorxiv.org/content/10.1...

I am thrilled to share that our manuscript on using LEA proteins to prevent air-water interface damage to fragile samples for cryo-EM is officially out! #CryoEM doi.org/10.1038/s414...

1/3: Led by @kaitlynabe.bsky.social, we found small LEA proteins from nematodes and tardigrades (water bears!) to be incredibly effective in protecting two test fragile complexes - human DNA polymerase alpha-primase and polycomb repressive complex 2 - from AWI damage during plunge freezing.

Exhausted with trying multiple ways to combat the air-water interface (AWI) problem during sample grid plunge freezing? We may have an easy solution for you! Read our latest preprint on how we use LEA proteins as AWI sample protectants for challenging samples: www.biorxiv.org/content/10.1...

I am excited to share that my work with @cijilim.bsky.social on protecting fragile samples from air-water-interface damage during cryo-EM plunge freezing is in preprint! www.biorxiv.org/content/10.1...