Lorenz Grundmann

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.

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...

Congratulations Juan. Really amazing 🤩

Fair.
It is just easier for me to believe that someone tries to get away with something like this than someone actually getting away with it (for now at least). Mind boggling.

Whatever happened here cannot be called peer review imo. I don't know who did worse - the authors or the "reviewers". They even show the frickin map in a main figure.
Crazy that many excellent papers in Structure have to stand next to something like this.

Figure 1 from the preprint

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

... or a 30S proteasome.

The last one looks like a 26S proteasome (~350Å long) to me. The one before that also seems to be a proteasomal assembly. Hard to say which one but could be a hybrid proteasome (19S one one side of the 20S and PA200 or PA28 on the other side).

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

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...

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)

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...

Makes sense, thanks for the explanation 🙂

Looking forward to play around with it once available on EMPIAR. It seems ideal to get a grasp on the processing of (pseudo)symmetric complexes with symmetrie breaking interaction partners.

I was surprised to see that the classification was that complicated. Did you try refinement and 3D classifications with or without image alignment in C1 before refining in C16?
Either way this is such a cool processing problem resulting in such a cool structure and story.
Much congrats!

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/...

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 ...

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...

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...

If you are thinking about the future of structural biology, we are too! Our two cents (Jürgen Plitzko and I) just got published online here: authors.elsevier.com/sd/article/S...

📄 New paper: 3DEM Structure Map Validation Recommendations

Two new metrics assess model-to-map fitness in cryo-EM:
🔹 Q_relative_all → compares avg Q-score across PDB/EMDB
🔹 Q_relative_resolution → compares within similar resolution

#3DEM #CryoEM #wwPDB

We’re hosting the @embo.org Practical Course on In-situ structural biology by CryoFIB and CryoET in April 2026! 🧬❄️ You can expect hands-on training, cutting-edge methods, and a chance to work alongside leading experts in structural biology. 🔗 Apply by Dec 8, 2025: meetings.embo.org/event/26-in-...

Integrated structural biology of the native malarial translation machinery and its inhibition by an antimalarial drug Nature Structural & Molecular Biology - Integrated structural biology approach leveraging in situ cryo-electron tomography reveals molecular details of the native malarial translation...

Our #CryoET story on how a top antimalarial drug candidate perturbs the native malarial translation machinery is out @natsmb.nature.com🥳 rdcu.be/eBbrH

A massive team effort led by @leonieanton.bsky.social Meseret Haile & Wenjing Cheng in collaboration with Jerzy Dziekan & the Alan Cowman! #TeamTomo

Very nice, congratulations "Danger" Daniel 😆

A rapid, simple, and economical method for the isolation of ribosomes and translational machinery for structural and functional studies Nature Communications - Here, the authors present a method to rapidly isolate actively translating ribosomes in a time- and cost-effective manner using poly-lysine. The method is compatible with a...

Our RAPPL purification of ribosomes and associated material is out. I am really proud of this study in collaboration primary with Pavlovic-Djuranovic lab, as well as Jovanovic and Hashem Labs. This method aims to replace 60 years old purification of ribosomes by sucrose cushions

rdcu.be/ezlhg

Come join us for the Austrian Cryo-EM Symposium!

That's a wrap! The results of the first #cryoEM heterogeneity challenge are up on biorxiv!
biorxiv.org/content/10.110

Very cool, congratulations! I was waiting for this 😄
Seems like I will have to compare my favorite methods 🎉

1/10 Today in @science.org in collaboration with
the Liu group we report the development of a laboratory-evolved CRISPR-associated transposase (evoCAST) that supports therapeutically relevant levels of RNA-programmable gene insertion in human cells. drive.google.com/file/d/1I-Ub...

Congrats to @lgrundmann.bsky.social for winning a poster award at #EMBORNAmeetsproteindecay

The 'RNA meets Protein Decay' @embo.org workshop was really a blast. Thanks to everyone for the lively discussions!
I am especially honoured that my poster was awarded with one of the two poster prizes 😇

The 2nd edition of the @embo.org workshop 'RNA meets Protein Decay', this time here in Vienna @impvienna.bsky.social, came to an end. Thanks to everyone who came and contributed to the great vibe of sharing science, discussing ideas and connecting with each other!