#cryoEM enthusiast now also at @haselbachlab@mstdn.science
Wien, Österreich
Joined January 2011
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New Preprint: We have solved the structure of the proteasome in complex with two different ubiquitin chains: biorxiv.org/content/10.1101/… This work spearheaded by PhD Student Sascha Amann
Let me walk you through it 🧵 1/9
I am so proud of Sascha! If you want to know about his amazing work that led to this award check out his two preprints: biorxiv.org/content/10.1101/… biorxiv.org/content/10.1101/…
Sascha Amann won the 2026 Rabitsch Award! 🏆 A recent PhD graduate from the CryoEM Technology Platform, Amann received the award for his research on how the proteasome recognises and degrades proteins tagged with ubiquitin: bit.ly/4hQTCs1
Haselbach lab retweeted
The annual Cryo-EM Symposium took place on Campus this year. It is collaboratively organized by the Vienna BioCenter & ISTA and aims to explore & celebrate the latest advancements in Cryo-EM research & its impact on biological studies. Thank you to everyone joining!
Last call: registration for the 9th Austrian Cryo-EM (ACE) Symposium closes TOMORROW, 1 Sept. 24-25 Sept at @IMPvienna.
Speakers: @CostaLabCrick @DemulderManon @DanielHurdiss @ZhongingAlong, Petr Chlanda, Zhaoming Su, Katarina Toropova, Gregor Weiss
events.vbc.ac.at/imp_events/…
🔬 Announcing the 9th Austrian Cryo-EM (ACE) Symposium! Sept 24-25, 2026 at IMP, Vienna.
📝 Abstract deadline: Aug 5 (Several speakers will be selected from abstracts)
🔗 Register: imp.ac.at/research/cryo-em-s…
#CryoEM
Haselbach lab retweeted
I have stopped posting on social media, but this is a special occasion. I am glad to share that our work has been published in Science Advances! We made it work through great collaborations with outstanding colleagues. science.org/doi/10.1126/scia…
Here is a video summary of our recent paper (nature.com/articles/s41467-0…) on the nuclear transport of the proteasome: youtube.com/watch?v=eNY2CRlY…
This way the proteasome can pass the nuclear pore barrier. Inside the importins are released and Akirin2 is degraded by the proteasome itself.
This work was spearheaded by @HannaBrunner_ and is a collaboration with the Johannes Zuber lab. It features a saturation mutagenesis screen, a cryoEM structure of the import complex and a invitro reconstitution of the nuclear import process
Haselbach lab retweeted
To regulate gene activity, proteasomes - waste disposal machines of cells - must enter the nucleus. IMP Researchers now show how the adaptor protein AKIRIN2 helps ferry this massive complex through the nuclear pore: nature.com/articles/s41467-0…
Haselbach lab retweeted
We introduce a new method, EmbedOpt, for robustly steering protein sequence-to-structure diffusion models to fit experimental data (Cryo-EM, NMR) without training. 🧬📉 @mhli41 @JiequnH @PilarCossio2
EmbedOpt tackles the brittleness of the previous coordinate-space steering methods by optimizing the conditional embedding instead. These embeddings capture rich co-evolutionary signals in protein diffusion models—unlocking a new, robust and semantically meaningful diffusion steering axis.
🚀 Result: Better fitting, wider hyperparam stability, and efficiency enabled by fewer diffusion steps
📄 Preprint: arxiv.org/abs/2602.05285
Haselbach lab retweeted
Sven Klumpe, joint Group Leader at the IMP and IMBA has received a grant by the Chan Zuckerberg Initiative’s Biohub to support fibsem-os, an open-source software platform for focused ion beam–scanning electron microscopy.
Read more 👉 imba.science/4tiwEP9
Haselbach lab retweeted
New work from our Haselbach lab with collaborators captures ribosomes 𝘮𝘪𝘥-𝘣𝘶𝘪𝘭𝘥 and reveals a flexible, modular strategy behind their assembly, rather than a strict assembly line.
Published in _Nucleic Acids Research _👉 doi.org/10.1093/nar/gkag036
the 4th paper in this week contribution from our lab tells about ribosome biogenesis in yeast. A follow-up story from our wonderful collaborators @UniGraz - the Bergler Lab. Structural work was again done by the amazing Lorenz Grundmann
academic.oup.com/nar/article…
Happy I could contribute to this amazing story. Finally visualizing the activity of single proteasomes within cells a real dream come true. Check the preprint biorxiv.org/content/10.64898…
New lab paper!! We develop a technology for live-cell, single-molecule visualization of proteasomal substrate degradation. We find that the site of substrate engagement by the proteasome determines decay kinetics, efficiency and co-factor requirement.
biorxiv.org/content/10.64898…
And another paper with our contribution. Sascha Amann managed to gain structural insights from this incredible hard to analyse cryo EM. Full story at: pnas.org/doi/10.1073/pnas.25…
BLOC-1 and BORC help move and position lysosomes inside cells. New work from the Haselbach and Clausen labs shows they are not uniform complexes, but families of related protein assemblies. Published in PNAS: pnas.org/doi/10.1073/pnas.25…
Have a look at our new structure of co translational folding in yeast. This is collaborative work initialized by the Rospert lab from the @UniFreiburg . Structural work has been done by the amazing Lorenz Grundmann.
🧪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: nature.com/articles/s41467-0…
Haselbach lab retweeted
🌍Open call: Junior Group Leader positions!
Join a world-class biomedical research institute at the heart of the Vienna BioCenter, where curiosity drives discovery.
Lead your own lab, pursue bold ideas, and shape the future of science at the IMP: imp.ac.at/career/open-positi…
Haselbach lab retweeted
How do cells decide on the life or death of a protein?
🔬 Researchers around @HaselbachLab at the IMP have captured the first high-resolution view of the human proteasome reading different ubiquitin signals.
➡️Read the full story: imp.ac.at/news/article/how-c…
This was a great team effort and we thank our Funders: @Boehringer, @FWF_at , WWTF, @ERC_Research , the @NIH. We also thank for the great support of the @IMPvienna and the help of the great facilities @VBCF_Tweets 8/9
Similar results have been obtained earlier this year by @PDraczkowski et al. using a different kind of K11/K48 branched chain. See also their preprint: biorxiv.org/content/10.1101/… 9/9