🆕 publication! How do cells build their molecular machines? Tsimafei Navalayeu (Ameres lab) in @embojournal.org maps the stepwise assembly of the RNA exosome in mammalian cells, revealing the quality control mechanisms that ensure this essential complex is built correctly ➡️ tinyurl.com/84c2298e

Not wanting to be snarky but this is true of every technological advance in science. My entire PhD in 1983 was the fitting and refinement of a single protein crystal structure. Today I could do the same within an hour - no AI required. Hyperbole does not help.

Research Professional News@resprofnews.bsky.social · 2mo ago

Artificial intelligence systems will allow a single PhD student’s output to match that of a whole laboratory, according to Demis Hassabis, a Nobel laureate for chemistry.

Super cool cryo-ET work from my colleague Xiaohan resolving a ton of ribosome assembly intermediates in the nuclei of human cells!

bioRxiv Cell Biology@biorxiv-cellbio.bsky.social · 2mo ago

In-cell structures visualize human pre-ribosome assembly in the nucleolus https://www.biorxiv.org/content/10.64898/2026.06.01.729245v1

For years, the #cryoEM community viewed ~50 kDa as the practical lower size limit for SPA. This was challenged by Kim et al., who introduced the HR-HAIR method and demonstrated structure determination of proteins below 30 kDa using #CryoSPARC. Read more 👉 bit.ly/3RHMxAt

CryoSPARC | The Resolution Revolution Is Still Ongoing

High-Resolution Ab-Initio Reconstruction: Extending Cryo-EM to Smaller Particles with CryoSPARC™

bit.ly

Try this new online training game from Leandro F. Estrozi designed for newcomers in structural biology, with a focus on cryo-EM and cryo-ET map interpretation: rico.ibs.fr/helixplo...

We're super excited to share MissAlignment: a new ML-based approach to reference-free tilt series alignment, spearheaded by @martenchaillet.bsky.social. We think it's going to make your cryo-ET life a lot better. Preprint: www.biorxiv.org/content/10.6... Code: github.com/warpem/miss-... 🧶 Thread:

Cells have a built-in cleanup system to remove unwanted proteins, and scientists can hijack it to destroy cancer drivers. Now, researchers from our Haselbach lab and collaborators reveal how this works in near-atomic detail: https://www.nature.com/articles/s41467-026-72235-9

Check out the final version of this work, out today! @natcomms.nature.com www.nature.com/articles/s41...

Ahmad Jomaa@jomaalab.bsky.social · last yr.

Check out our new preprint on the discovery of a molecular switch in NAC that mediates nascent chain sorting on the ribosome and prevents mitochondrial protein mistargeting by SRP. A great collaboration with the Shan Lab @Caltech and the Qi Lab @UVA: www.biorxiv.org/content/10.1...

Happy to share my first adventure in #TeamTomo in collaboration with the talented @inaharasimov.bsky.social. It was a fun experience experience with a lot of learning along the way.

Carter Lab@carter-lab.bsky.social · 4mo ago

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...

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...

I am incredibly excited to share that I will start my independent lab at the @unidue-zmb.bsky.social at the @unidue.bsky.social as Junior Professor of Cellular Biochemistry. Research in my lab has the goal to decipher the ubiquitin code! There are multiple open positions! (1/3)

Long in the making, but happy to present the Chlamydomonas chlororibosome! Cryo-ET🔬reveals a large new domain on the small subunit, built from multiple extensions in conserved ribosomal proteins. bioRxiv 📖: shorturl.at/q44tG This suggests greater chlororibosome diversity than expected! 1/n 🧵

Please share! My group at @zmbp-tuebingen.bsky.social is offering a post-doctoral position (4 years). We look for a structural biologist with experience in Cryo-EM/Cryo-ET to investigate the mechanisms of host invasion by pathogenic fungi. Deadline February 28th! uni-tuebingen.de/universitaet...

Formation & function of #MembranelessOrganelles! #CryoET structures of #proteasome storage granules inside cells! Read our paper @cp-cell.bsky.social! ❕Publication: doi.org/10.1016/j.ce... ❕Press Release: www.biochem.mpg.de/en/pressroom @uoftmedicine.bsky.social @erc.europa.eu #UPSmeetMet

Check out our new paper in @natcomms.nature.com .com where we used #cryoEM together with biochemical and mutational analyses investigated the cotranslational protein folding by Ssb in yeast. Publication: doi.org/10.1038/s41467-025-67685-6 Check below for the cryoEM centric feed. 👇

Have a look at our new structure of co translational folding in yeast. This is collaborative work initialized by the Rospert lab from the @uni-freiburg.de. Structural work has been done by the amazing @lgrundmann.bsky.social Stay tuned for the next ribosome paper from him, following very soon.

IMP@impvienna.bsky.social · 7mo ago

🧪Scientists from our Haselbach lab captured how proteins begin to fold as they’re being made. Using cryo-EM, they visualised chaperones guiding nascent proteins on the ribosome: https://www.nature.com/articles/s41467-025-67685-6

And the 4th paper in this week contribution from our lab tells about ribosome biogenesis in yeast. A follow-up story from our wonderful collaborators in Graz - the Bergler Lab. Structural work was again done by the amazing @lgrundmann.bsky.social: academic.oup.com/nar/article/...

A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation

Abstract. Formation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) whil

academic.oup.com

One month later and still thinking about the great science and conversations from the 8th Austrian Cryo-EM Symposium 🧊🔬 Huge thanks to all who joined - let’s make next year even bigger! cryoem-symposium.pages.ist.ac.at/invited-spea...

New paper alert! Scientists in Clemens Plaschka’s lab at the IMP and @juliusbrennecke.bsky.social's lab at @imbavienna.bsky.social solved a decade-old puzzle, uncovering how the information molecule mRNA travels from the cell’s nucleus to its periphery. More: bit.ly/4nHcvys

just in time for the opening of the @hohmannulrich.bsky.social group at @imbmainz.bsky.social what started as a project on how cells export piRNA precursors, ended up as a tour de force in mRNA export. truly wonderful collaboration with @plaschkalab.bsky.social at the @viennabiocenter.bsky.social

IMP@impvienna.bsky.social · 9mo ago

New paper alert! Scientists in Clemens Plaschka’s lab at the IMP and @juliusbrennecke.bsky.social's lab at @imbavienna.bsky.social solved a decade-old puzzle, uncovering how the information molecule mRNA travels from the cell’s nucleus to its periphery. More: bit.ly/4nHcvys

My main work as postdoc @plantophagy.bsky.social lab in @gmivienna.bsky.social is out in @natplants.nature.com 🌱🎉 We asked how can protein complexes diversify without compromising their function and explored this question using the plant #exocyst complex. www.nature.com/articles/s41...

Electrostatic changes enabled the diversification of an exocyst subunit via protein complex escape - Nature Plants

The evolutionary diversification of an exocyst subunit was enabled by electrostatic shifts leading to its dissociation from the ancestral complex.

nature.com

Check out our preprint! With new molecular mechanisms, 140 subtomogram averages, and ~600 annotated cells under different conditions, we @embl.org were able to describe bacterial populations with in-cell #cryoET. And there’s a surprise at the end 🕵️ www.biorxiv.org/content/10.1... #teamtomo

Thrilled to share that I’ll be joining @imbmainz.bsky.social in February 2026 to start my own group! We will explore new mechanisms in eukaryotic gene expression, leveraging ‘evolutionary play’ to uncover how regulation, repurposing, and hijacking shape RNA biology. PhD positions available!

Join us for the Austrian Cryo-EM Symposium from Nov 11–12 at ISTA! Top speakers, cutting-edge cryo-EM, and a chance to explore Vienna & the ISTA campus. Register now 👉 cryoem-symposium.pages.ist.ac.at/registration/ #cryoEM

A good day to remember John Gurdon’s school report from his biology master at Eton

How are RNAs sorted for export vs. degradation in the nucleus? In collaboration with @heick.bsky.social’s lab we (@clemensplaschka.bsky.social and @juliusbrennecke.bsky.social labs) discovered a direct mechanistic link between the export and decay machineries: www.biorxiv.org/content/10.1... (1/x)

Molecular basis of polyadenylated RNA fate determination in the nucleus

Eukaryotic genomes generate a plethora of polyadenylated (pA+) RNAs[1][1],[2][2], that are packaged into ribonucleoprotein particles (RNPs). To ensure faithful gene expression, functional pA+ RNPs, in...

biorxiv.org

I am excited to announce that I will be moving to IMB Mainz next year! The Winter call for the IPP PhD program is now open; if you are interested in maternal #mRNA regulation and #translation in early vertebrate development, please apply! Deadline: 16 October. More info: www.imb.de/students-pos...

Glad to share the final version of our story about the UBR4 complex, an E4 ligase protein quality control hub @science.org. Now with more cryo-EM structures and a deeper dive into substrate recognition, especially escaped mitochondrial proteins @clausenlab.bsky.social www.science.org/doi/10.1126/...

Happy to share our work on the structure and function of the unusual E3 ligase ZNFX1 @cp-cell.bsky.social. It uses a nucleic acid-activated transthiolation mechanism, ubiquitinating and clustering RNA to protect cells in an immune response. @clausenlab.bsky.social www.cell.com/cell/fulltex...

A split-site E3 ligase mechanism enables ZNFX1 to ubiquitinate and cluster single-stranded RNA into ubiquitin-coated nucleoprotein particles

Grabarczyk et al. show the structure and mechanism of a non-canonical ubiquitin ligase, which is activated through nucleic-acid-induced oligomerization and is critical for cell survival during immune ...

cell.com

Exciting to see our protein binder design pipeline BindCraft published in its final form in @Nature ! This has been an amazing collaborative effort with Lennart, Christian, @sokrypton.org, Bruno and many other amazing lab members and collaborators. www.nature.com/articles/s41...