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Our latest publication reports the cryo-EM structures of the human Polα-Primase DNA elongation complexes - rdcu.be/c96yY A Lim lab X Tahirov lab collaboration led by Qixiang He 贺琦翔 and Andrey. Thank you, Sara Osman & NatureStructMolBiol, for working with us! Please RT to share! 1/4

1/6: #CryoEM Exhausted with fighting 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: biorxiv.org/content/10.110…

2/6: Led by Kaitlyn Abe, we found small LEA proteins from nematodes and tardigrades (water bears!) to be incredibly effective in protecting two test fragile complexes - human DNA polymerase α-primase and polycomb repressive complex 2 - from AWI damage during plunge freezing.

3/6: The human DNA polymerase α-primase is a challenging complex to determine its structure. By simply adding nematode AavLEA1 protein to our complexes before plunge freezing, we achieved the highest-resolution cryo-EM map reported for the apo complex at 3 Å. #DNAReplication

4/6: Similarly for human PRC2, which is notoriously challenging to solve its cryo-EM structures - required crosslinking & surface adsorption, by adding LEA proteins before freezing, we determined cryo-EM maps of PRC2 at comparable resolutions to those previously reported. #PRC2

5/6: We think the LEA protein provides a simple, cost-effective, and readily deployable solution for cryo-EM SPA users to overcome their AWI sample issues. Any labs that can make proteins from E. coli can immediately incorporate this strategy into their existing pipeline. #AWI

6/6: We don't claim LEA proteins as a universal solution as we can't test every challenging sample in our lab. So please feel free to reach out if you wish to test these LEA proteins for your samples. Very happy to send some over! We like to see you revive your 'dead' projects!

I am super excited to share that my first manuscript with Ci Ji Lim on protecting fragile protein complexes from air-water-interface damage during cryo-EM plunge freezing is in preprint! biorxiv.org/content/10.110…

Organisms like nematodes and tardigrades (water bears) have evolved proteins to protect their cells from freezing and dessication. We have found that these proteins can also shield cryo-EM samples from damage at the air-water interface.

1/7 Our latest preprint is out! 🚨 Sourav Agrawal | ସୌରଭ , Xiuhua Lin , Vivek Susvirkar et al. discover human RPA is a critical telomerase processivity factor essential for telomere maintenance. This reshapes our understanding of human telomerase regulation. biorxiv.org/content/10.110…