Chris Lupton

Very well deserved! A great reward for a a lot of hard work 😊

Seed to sub-Å!
We just solved crambin at 0.85Å with #MicroED straight from spontaneous nanocrystals, phased ab-initio from a 5-res helix. Video shows diffraction ➜ ugly start map ➜ beautiful spheres. Preprint: www.biorxiv.org/content/10.1...
#StructuralBiology #CryoEM

Awesome talk from @bradleyspicer.bsky.social telling us all about his work on insecticidal proteins. Very cool stuff! #lorneproteins2025

🚨 Save the Date! 🚨

I'm thrilled to announce the Prato Conference on Pore Forming Proteins, happening this June in the stunning city of Prato, Italy!

🙏 Please share or repost this to help us reach as many people as possible—especially those who would love to attend!

Dynamic PRC1–CBX8 stabilizes a porous structure of chromatin condensates - Nature Structural & Molecular Biology Here the authors show that a gene-inactivating protein complex packs inactive genes into a dynamic and accessible structure. The study challenges the traditional views that restricted accessibility an...

We used cryoET and biophysical approaches in vitro together with molecular biology in differentiated cells to show that chromatin compacted by PRC1-CBX8 is porous and accessible while PRC1 is dynamic in it. 🧪🧬 #cryoET #Epigenetics #Polycomb www.nature.com/articles/s41...

🧵 1/ We’re excited to share that our new paper with @adrianbracken.bsky.social lab is out 🎉 In this study (which began over 10 years ago!), we explore the biology of PRC2 and PRC1 in non-dividing cells. We also explore the effects of PRC2 inhibitor drugs on these cells. Here’s what we found👇

Agreed. I've had presenters/audience from the poster next to me stand in front of my poster. Not ideal...

Very cool! 😁

Structure of the human TSC:WIPI3 lysosomal recruitment complex The complete TSC structure reveals how lysosomal targeting proteins and phosphoinositides coordinate mTORC1 inhibition.

Great to see our work on the #cryoem structure of the human TSC:WIPI3 lysosomal recruitment complex! Awesome effort from co-authors @charlesbj.bsky.social and Laura D'Andrea with @drellisdon.bsky.social doing the heavy lifting leading the project.

www.science.org/doi/10.1126/...

Our latest study is now online at Science Advances! We report the structure of the gigantic TSC:WIPI3 complex revealing new insights into lysosomal docking and dysregulation in disease. #cryoEM #mTOR 🧪

www.science.org/doi/10.1126/...

LYCHOS is a human hybrid of a plant-like PIN transporter and a GPCR - Nature Cryo-electron microscopy structures of the human lysosomal transmembrane protein LYCHOS show that it comprises a transporter-like domain fused to a G-protein-coupled receptor, and that the transporter...

Excited to see our latest study published!

We report several structures of the intriguing LYCHOS (GPR155) protein revealing a chimeric structure of a GPCR and a PIN-like transporter domain #cryoEM #mTOR #GPCR #auxin

www.nature.com/articles/s41...

🚨 Our story on the TSC:WIPI3 lysosomal-recruitment complex is now live in Science Advances.

Equal-first co-authors @luptoncj.bsky.social & Laura D'Andrea. Work lead by @drellisdon.bsky.social. Funding from @deptofdefense.bsky.social & Australian Research Council.

www.science.org/doi/10.1126/...

Bound by the love for cholesterol: A transporter meets a GPCR In a recent issue of Nature, Bayly-Jones et al. report the cryo-EM structures of a lysosomal cholesterol sensor, LYCHOS, also known as GPR155, which reveals a unique fusion of a plant auxin-transporte...

Another really nice highlight of our recent work. Arun et al raise interesting points about membrane cross talk and next-steps for LYCHOS. www.cell.com/cell/abstrac...

Thanks! It really was very cool and there's still so much more to discover!

Very cool to see our work on the #cryoEM structure of LYCHOS as the Editor's Choice in Science Signalling! Thanks @jffoley.bsky.social !!