This lateral engagement positions NetF close to the membrane, enabling direct lipid contacts and pore insertion, possibly a conserved strategy among clostridial hemolysin β-PFTs. With Chang Wang, Filippo Cattalani, Ioan Iacovache (@coldpopeye.bsky.social), Horst Posthaus, and colleagues.

Using cryo-EM, we solved the NetF pre-pore, pore, and co-structure with ANTXR2. Although NetF and anthrax PA share the same receptor, their binding modes differ completely: NetF engages ANTXR2 laterally across vWA and Ig-like domains, while PA targets the apical MIDAS motif.

Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor - Nature Communications This study identifies ANTXR2 as the cellular receptor for Clostridium perfringens toxin NetF and determines its structure bound to the toxin using cryo-EM, revealing a distinct lateral binding mechani...

New paper in Nature Communications: we identified ANTXR2 (CMG2) as the cellular receptor for C. perfringens NetF toxin, causing hemorrhagic enteritis in dogs and foals. ANTXR2 was previously known as the receptor for anthrax toxin PA. doi.org/10.1038/s414...

Genetically encoded FerriTag as a specific label for cryo-electron tomography Wang et al. present an optimized labeling strategy for cryo-electron tomography based on genetically encoded FerriTag. This system uses rapamycin to recruit iron-loaded ferritin to target proteins, en...

Paper alert🚨
Label your protein of interest and localize it in cryoET 👁️❄️

Genetically encoded FerriTag as a specific label for cryo-electron tomography: Structure www.cell.com/structure/fu...

We are hiring-join us!

In collaboration with the Posthaus Lab, we identify ANTXR2—also the anthrax toxin receptor—as the receptor for Clostridium perfringens NetF pore forming toxin. Cryo-EM shows extensive contact between the pore and the receptor
🧬🧊🔬 #Microbiology #CryoEM #PoreFormingToxins
doi.org/10.1101/2025...

Near-atomic detail from large sample areas using cryo-EM of frozen biological sample slices This study explores how cryo-electron microscopy (cryo-EM) can be used to image large areas of frozen biological samples with near-atomic resolution. The researchers used a method called CEMOVIS, whic...

A plain language overview of our recent publication link.growkudos.com/1bt0psurksg

Out now at IUCJ doi.org/10.1107/S205...

Happy to announce our latest preprint. High resolution ribosomes in cells obtained on CEMOVIS (frozen-hydrated sections) www.biorxiv.org/content/10.1... in collaboration with @grigoriefflab.bsky.social and Wanda Kukulski.

www.biorxiv.org/content/10.1...

NEW PREPRINT ALERT!
Thanks to all involved!

Cryo-EM structure of a phosphotransferase system glucose transporter stalled in an intermediate conformation The phosphotransferase system glucose-specific transporter IICBGlc serves as a central nutrient uptake system in bacteria. It transports glucose acros…

Please check out our latest cryo-EM structure in the Journal of Structural Biology X: Structure of the PTS glucose transporter IICB stalled in an intermediate conformation.

www.sciencedirect.com/science/arti...

Congratulations Patrick for this great work !

Ingo Greger sat in front of a computer screen displaying an AMPA Receptor structure

Great position for a postdoc to join @igreger.bsky.social’s group in the LMB’s Neurobiology Division, using diverse methods to study synaptic AMPA glutamate receptors.
Read more about the job here: www.nature.com/naturecareer...
Apply by 20 FEB
#PostdocJobs #ScienceJobs

Come and set up your own group at the @mrclmb.bsky.social in Cambridge, UK. Feel free to chat/email me with questions.

Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment Aerolysin is a β-pore-forming toxin produced by most Aeromonas bacteria, which has attracted large attention in the field of nanopore sensing due to its narrow and charged pore lumen. Structurally sim...

Our latest JACS paper: high-resolution cryoEM of #aerolysin in lipid environment shows pore properties and 4 key constriction rings for #nanopore sensing. Collaboration with #DalPeraro & #Cao labs.
@coldpopeye.bsky.social
@unibern.bsky.social
#EPFL #UNIGE #DubochetCenter #MIC
shorturl.at/qyzbb

🎉Our latest publication "Predicting Polypharmacology with Web-Based Tools" by @maedehdarsaraee.bsky.social, Sacha Javor, and Jean-Louis Reymond is now published on Wiley!
Read it here👉
onlinelibrary.wiley.com/doi/abs/10.1...

#DCBP
#polypharmacology
#target_prediction
#chembl
#fingerprint
#ML

Now hiring: Research Group Leader To join the LMB’s Neurobiology Division and develop an independent research programme in the field of molecular connectomics, supported by core funding, excellent research facilities, and a lively community of colleagues. Apply by 19th January 2025. Background shows a connectomic map of an adult fly brain.

Reminder:
Outstanding opportunity to open your group in the LMB’s Neurobiology Division as part of our Molecular Connectomics Initiative!

You will be supported by core funding, excellent facilities and a lively international community of researchers.

Apply by 19 Jan

www.nature.com/naturecareer...

Our January cover shows a reconstructed synapse from a cryo-electron tomogram of cultured hippocampal neurons expressing a SNAP-25 mutant, using CryoVesNet developed by Amin Khosrozadeh, Benoît Zuber et al. (https://buff.ly/4h0DjGN
JCB's January issue is here ✨ https://buff.ly/3ZZLqwE