Added custom menus, including one to quickly add common monomers (detergents, buffers etc):

Excited to share our work on the structure and function of cytoplasmic lattices within mouse embryos. A collaborative effort with @niakanlab.bsky.social and work led by @kashishsingh.bsky.social and @inaharasimov.bsky.social . It is now out on BioRxiv: www.biorxiv.org/content/10.6...

Finally got around to porting my coot-trimmings scripts over to Coot 1... only the hotkeys are working (nothing requiring creating a custom menu or GUI dialog), but I've added a couple of new ones, e.g. copy/pasting ligands.

Check it out & let me know what you think! 😊

github.com/olibclarke/c...

Surface ice ruining your cryo-ET lamellae? We showed you can sublimate it away — inside the SEM, no extra hardware, no devitrification. 🧊→✨
New preprint from @KarolinskaInst 3D-EM 🧵👇

We're excited to announce the beta-release of #RELION-5.1! 🥳 This release has important updates on our #amyloid processing pipeline, as described in this preprint: doi.org/10.64898/202... There are also some tweaks for #teamtomo.

#OpenSoftwareAcceleratesScience

Cryo-EM image processing of amyloid filaments in RELION-5.1 www.biorxiv.org/content/10.64898/2026.03.17.712386v1 #cryoEM

You asked, we listened. Millions of AI-predicted protein complex structures are now available in the #AlphaFold Database.

This spans homodimers from 20 of the most studied species, including humans, as well as the World Health Organization’s priority pathogens list.

www.ebi.ac.uk/about/news/t...

AlphaFold database has entered the era of complexes. Together with NVIDIA, DeepMind and EBI, we use ColabFold, OpenFold and MMseqs2-GPU to predict ~31 million complexes (homo & hetro-dimers) resulting in 1.8 million high-quality predictions
📄 research.nvidia.com/labs/dbr/ass...
🌐 alphafold.ebi.ac.uk

In-Chamber Sublimation: A Practical Approach for Mitigating Ice and Curtaining in Cryo-Electron Tomography Lamellae Preparation www.biorxiv.org/content/10.64898/2026.03.12.711158v1 #cryoEM

Happy to share our new preprint on the mechanism of human tRNA 3' CCA maturation! This project was spearheaded by Bernhard Kuhle in my group, with contributions from many others and a great collaboration with the group of Peter Rehling (UMG). See highlights below!

www.biorxiv.org/content/10.6...

High-resolution in situ structures of hantavirus glycoprotein tetramers pubmed.ncbi.nlm.nih.gov/41763200/ #cryoEM

ChimeraX screenshot showing CubeNTube plugin.

The new ChimeraX CubeNTube plugin allows erasing parts of maps using cube, cylinder, and custom shapes and has undo. Created by Tamino Cairoli. Available from ChimeraX menu Tools / More Tools....

Since last year, I've been making a RELION GUI that supports viewing, navigating and running jobs in a way completely compatible with the original RELION pipeline. Now it's working nicely for both SPA and tomography! Please try it out - github.com/hanjinliu/hi...

The vault particle is enclosed by a C13-symmetric cap with a positively charged exterior pubmed.ncbi.nlm.nih.gov/41706843/ #cryoEM

Euler Hunt Can you find the Euler angles of a cryo-EM projection?

I had Claude make this as a mini-game for Relay's disconnect screen (like Chrome's dinosaur), but then pivoted to stand-alone. In this game, you have to find Euler angles matching the target projection, i.e. cosplay RELION. It can be pretty hard. Works on mobile too! warpem.github.io/euler-hunt/

🚀 CryoSPARC v5.0 BETA is here!

We’re excited to deploy another major #CryoSPARC release to help enable and accelerate #cryoEM data analysis. v5 has a redesigned underlying software system and many new features - highlights in thread!

Full changelog: cryosparc.com/updates/v5.0.0

IsoNet2 determines cellular structures at submolecular resolution without averaging www.biorxiv.org/content/10.64898/2025.12...

Und hier sind sie – die 10 Preisträger*innen des Gottfried Wilhelm #LeibnizPreis' 2026 – ausgezeichnet für ihre exzellenten Forschungsarbeiten und Errungenschaften in der Wissenschaft! 🏆👏
Die Verleihung der Preise feiern wir am 18. März in Berlin.
Einzelheiten & Kurzprofile: sohub.io/1uv1

Atomic models of the Toxoplasma cell invasion machinery Nature Structural & Molecular Biology, Published online: 09 December 2025; doi:10.1038/s41594-025-01728-wZeng et al. applied single-particle cryo-electron microscopy to native samples isolated from the human parasite Toxoplasma gondii, determining multiple structures of key components of the conoid, a cone-shaped organelle essential for host cell invasion.

New online: Atomic models of the Toxoplasma cell invasion machinery

Loop-mediated regulation and base flipping drive RNA cleavage by human mitochondrial PNPase pubmed.ncbi.nlm.nih.gov/41361968/ #cryoEM

Thank you Emma! ☺️

Star student & postdoc Kiarash Jamali is setting up his own group at the Ellison institute in Oxford. Join him for the most exciting machine learning research in structural biology and beyond!! 🤩 #ProudPI

KI researchers have captured the first detailed molecular snapshots of human polynucleotide phosphorylase in action, revealing how this essential mitochondrial enzyme degrades RNA through an elegant base-flipping mechanism. Published in @narjournal.bsky.social 🧪 #mitochondria doi.org/10.1093/nar/...

Loop-mediated regulation and base flipping drive RNA cleavage by human mitochondrial PNPase Abstract. Human polynucleotide phosphorylase (hPNPase), a trimeric exoribonuclease, is crucial for maintaining mitochondrial RNA metabolism, including the

For more details check out our publication here: doi.org/10.1093/nar/...

The PH1 and PH2 domain loops, which span the pore of hPNPase, adopt distinct, asymmetric conformations. Only specific loop arrangements allow a loop from a neighboring protomer to interact and stabilize a single active site, suggesting an additional regulatory layer.

A catalytic magnesium ion, together with the RNA 2´-OH group, initially helps align Pi with the RNA scissile bond in position 1. Upon nucleophilic attack, the Mg²⁺ transiently shifts into position 2, avoiding steric clash with Pi and stabilizing the reaction intermediate.

For cleavage, hPNPase flips the two 3′-terminal bases of the RNA substrate by ~180°. This base flipping relocates the RNA from the loading to the pre-catalytic state, positioning the scissile bond in close proximity to Pi.

hPNPase binds RNA substrates in a largely sequence-independent manner. 3´-end specificity is enforced in the loading state that maximizes protein-RNA interactions while sterically constraining the 3´-end. To proceed to catalysis, the 3´-end must flip into the pre-catalytic state.

Our structures show that ssRNA is threaded into the active site through the bottom, and not the top pore of the trimeric hPNPase assembly.

Using cryo-EM, we determined hPNPase structures in three key states:
1. Apo state bound to inorganic phosphate (Pi)
2. RNA-bound loading state
3. RNA-bound pre-catalytic state