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

Diversifying particle-orientation distributions in cryo-EM with LEA protein additives

Preferential orientation at the air-water interface (AWI) remains a persistent challenge in cryo-electron microscopy, often requiring extensive optimization or specialized grid preparation strategies....

biorxiv.org

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

Charles Bayly-Jones@charlesbj.bsky.social · 7mo ago

Thrilled to share our latest work @luptoncj.bsky.social @drellisdon.bsky.social @drmlhalls.bsky.social. Structure of the lysosomal KICSTOR-GATOR1-SAMTOR nutrient-sensing supercomplex. 🧪🔬#cryoEM Now online @cellpress.bsky.social. doi.org/10.1016/j.ce...

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/...

Human RPA is an essential telomerase processivity factor for maintaining telomeres

Telomerase counteracts telomere shortening by repeatedly adding DNA repeats to chromosome ends. We identified the replication protein A (RPA) heterotrimer as a telomerase processivity factor critical ...

science.org

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...

Small LEA proteins as an effective air-water interface protectant for fragile samples during cryo-EM grid plunge freezing

Sample loss due to air-water interface (AWI) interactions is a significant challenge during cryo-electron microscopy (cryo-EM) sample grid plunge freezing. We report that small Late Embryogenesis Abundant (LEA) proteins, which naturally bind to AWI, can protect samples from AWI damage during plunge freezing. This protection is demonstrated with two LEA proteins from nematodes and tardigrades, which rescued the cryo-EM structural determination outcome of two fragile multisubunit protein complexes. ### Competing Interest Statement The authors have declared no competing interest.

biorxiv.org

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...