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Tomas Pascoa

@tomaspascoa.bsky.social
846 followers 662 following 26 posts

Postdoc at the Schuller Lab - Synmikro Marburg 🇩🇪 Cryo-EM/ET of anaerobic CO₂ fixation

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Reposted by Tomas Pascoa
Sjors Scheres @sjorsscheres.bsky.social · 06/10/2026
We have 2 new preprints on @biorxivpreprint.bsky.social that describe reconstitution of #Alzheimers paired helical filaments in experimental model systems: one in human brain organoids and one in murine primary cultures. www.biorxiv.org/content/10.6... www.biorxiv.org/content/10.6...
biorxiv.org
Templated seeding induces the formation of Alzheimer paired helical tau filaments in human brain organoids
The prion concept postulates that seeded aggregation results in the recruitment of soluble protein monomers and their assembly into amyloid filaments with the same structures as those of the seeds. He...
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Vasilii Mikirtumov @vasiliimikirtumov.bsky.social · 24/09/2026
thrilled to share that my main phd project is finally out in @natcomms.nature.com we present high-resolution structures of RyR1 in native membranes across multiple functional states by both cryo-ET/StA #TeamTomo and SPA! paper: www.nature.com/articles/s41... and a thread below⬇️⬇️⬇️
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Caitie McCafferty @computingcaitie.bsky.social · 09/09/2026
I am looking for a lab manager for my group that I will be starting at the @fmiscience.bsky.social in February! We will use in situ structural biology to investigate dynamic ciliary processes. More info here —> bsky.app/profile/comp... #cilia #teamtomo #proteomics #protistsky
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Ricardo D. Righetto @lifeonthewedge.bsky.social · 08/09/2026
A wild publishing ride to get here... but finally! (first bioRxiv: January 5th, 2024 🙃) Amazing work from @lorenzlamm.bsky.social and colleagues 🤗 Special thanks to the community who jumped early on the boat, sharing feedback and training data to make MemBrain v2 a reality 🙏🏽
nature.com
MemBrain v2: an end-to-end tool for the analysis of membranes in cryo-electron tomography - Nature Methods
MemBrain v2 enables streamlined analysis of membranes in cryo-electron tomography by providing user-friendly tools for membrane segmentation, membrane protein localization and spatial analysis, suppor...
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Ben Engel @cellarchlab.com · 28/07/2026
The final version of @florentwaltz.bsky.social's Chlamy chlororibosome "hat" is now online at @natplants.nature.com 🌾 📜 nature.com/articles/s41477-026-02361-1 🧪🔬 #TeamTomo The charge complementarity in the arm domain is striking. Blue & red proteins wrapped around each other, like a barber pole💈
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Ben Engel @cellarchlab.com · 18/06/2026
OK— so @phaips.vd.st & @florentwaltz.bsky.social have been testing extensively, and it's pretty clear that MissAlignment may be the best thing to happen to #TeamTomo in the last couple years. One issue: we have to re-process all our data again, hopefully for the last time 😅. Congrats and THANK YOU!!
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Danielle Grotjahn @nanigrotjahn.bsky.social · 16/06/2026
Cryo-ET is often framed as a tool for in situ protein structure. But what if the real revolution is contextualization? I explore how #teamtomo is redefining what "local" means in organelle biology, revealing membrane states rather than just protein structures. tinyurl.com/localmembrane
sciencedirect.com
Think globally, act locally: Redefining organellar membrane environments through cryo-electron tomography
Early enthusiasm for the “cellular revolution” in cryo-electron tomography (cryo-ET) was largely driven by the promise of resolving protein structures…
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Marcel Dickmanns | 🌿❄️🔬 @madic.bsky.social · 14/05/2026
It's out! 🥳 In situ architecture of #plasmodesmata - plant cytoplasmic bridges - by #cryoET. 📝 Paper: www.nature.com/articles/s41... 🧵 Thread: bsky.app/profile/madi... #teamtomo #proteomics #AlphaFold
nature.com
In situ architecture of plasmodesmata in Physcomitrium patens resolved by cryo-electron tomography - Nature Plants
Using cryo-electron tomography, the authors reveal how plasmodesmata (plant cytoplasmic bridges) are gated by cell wall remodelling and how helical protein assemblies scaffold internal membranes, with...
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Tomas Pascoa @tomaspascoa.bsky.social · 14/05/2026
Super cool work! Congratulations, Higor!
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Higor Rosa @hvdrosa.bsky.social · 14/05/2026
Thrilled to share the updated video of my paper in Nature with Maciej (under supervision of @simonemattei.bsky.social & @jomaalab.bsky.social) Proud to use Cryo-ET to uncover how hibernation factors are key to translation restart! To model PTMs in situ and render animations fulfilled my PhD dream!🥹🎉
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Tanmay Bharat @tbharat-lab.bsky.social · 07/05/2026
Oxygen gradients reshape cross-feeding through emergent spatial organization of gut commensal bacteria www.biorxiv.org/content/10.6... Use of isotope labels and cryo-CLEM-FIB-SIMS to study microbial communities by Hannah Ochner. Collaboration with @kiranrpatil.bsky.social @jmghigolab.bsky.social
biorxiv.org
Oxygen gradients reshape cross-feeding through emergent spatial organization of gut commensal bacteria
Microbial interactions unfold within environments structured by physical transport and chemical gradients. Yet most mechanistic studies rely on well-mixed systems that mask the reciprocal influences of environmental heterogeneity on metabolism and ecology. Here, we investigate how the physical environment modulates the interaction between the gut commensal Bacteroides thetaiotaomicron and Escherichia coli . In anoxic liquid culture, cell-resolved isotope imaging and genetic perturbations reveal exploitative cross-feeding, where E. coli consumes diffusible sugars released by B . thetaiotaomicron during starch degradation. When exposed to intestinal-like oxygen gradients in microfluidics, the interaction is restructured by spatial organization. The species self-organize into complementary niches: E. coli locally depletes sugars and oxygen, thereby expanding the anoxic niche required by B. thetaiotaomicron . A reactive transport model confirms that this organization arises from coupled feedback between physical transport and metabolic reaction rates. Together, our results reveal how physical structure and chemical gradients convert an exploitative cross-feeding interaction into a dynamic niche-construction process that generates emergent spatial organization and stabilizes coexistence. ### Competing Interest Statement The authors have declared no competing interest.
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Helena Watson @helenawatson.bsky.social · 25/04/2026
Preprint 🧵! I’m really excited to introduce BIGSMALL, an interleaved multi-magnification cryo-ET scheme bridging molecular and cellular scales in a single acquisition! BIGSMALL = 𝐁road 𝐈nformation 𝐆athering 𝐒trategy by 𝐌ultiscale 𝐀cquisition of lame𝐋𝐋a www.biorxiv.org/content/10.6... (1/6)
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joe dobbs @joedobbs.bsky.social · 22/04/2026
Big news for correlative cryogenic SMLM/ET! With my colleague Soheil, we (Mahamid and @jonasries.bsky.social labs) indicate lamella-specific illumination can allow 500-1500x higher laser intensities, opening massive new possibilities for correlative imaging #teamtomo www.biorxiv.org/content/10.6...
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joe dobbs @joedobbs.bsky.social · 22/04/2026
See also our preprint about the microscope itself, which went up earlier this afternoon! www.biorxiv.org/content/10.6...
biorxiv.org
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James Lingford @jameslingford.bsky.social · 15/04/2026
Amazing paper. A megadalton enzyme complex that: - combines both electron bifurcation AND confurcation steps - has a new type of iron-sulfur cluster - a new kind of weird electron transfer path - super charges electrons to reduce aromatic rings - also powers respiration 😳
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Tomas Pascoa @tomaspascoa.bsky.social · 15/04/2026
Thanks, Ricardo! We were super lucky to be able to work with Matthias and Lena on such a crazy project! It was really a fantastic team effort and, for me personally, a great opportunity to learn from you all! Thanks for your support along the way! 🤗
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Lars-Anders Carlson @lacarlson.bsky.social · 15/04/2026
Mother Nature is still the undisputed Queen of organic chemistry!
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joe dobbs @joedobbs.bsky.social · 14/04/2026
We @embl.org wrote a short preprint about optimizing for maximum completeness in #cryoet analysis. We looked at template matching, VPP imaging, and tilt-series refinement parameters, and why averaging ribosomes helps even if you aren’t interested in their biology 🏭 www.biorxiv.org/content/10.6...
Figure 4 from the preprint
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Anuj @rnfr2d2.bsky.social · 14/04/2026
How do “LEGO-like” electron-bifurcating modules combine to drive degradation in BTEX-contaminated ecosystems? Check out our latest preprint, where we use cryo-EM and cryo-ET to reveal how the 1 MDa BCRII complex powers extremely endergonic aromatic ring reduction. www.biorxiv.org/content/10.6...
biorxiv.org
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Ben Engel @cellarchlab.com · 14/04/2026
Across scales from cells🦠 to atoms⚛️ – We reveal how anaerobic #bacteria break down very stable aromatic compounds found e.g. in oil spills 🛢️ #Bioremediation #TeamTomo 🧪 🧶🧬 🔬 Awesome collab with Lena, Matthias, @schullerjm.bsky.social @rnfr2d2.bsky.social @tomaspascoa.bsky.social @tamb-o.bsky.social
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
8/ This was a really fun collaboration! Congrats to all co-first authors: Lena Appel from Matthias Boll’s lab, @rnfr2d2.bsky.social and me from @schullerjm.bsky.social, and @tamb-o.bsky.social from @cellarchlab.com!🎉
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
7/ Together, this work shows how evolution can expand metabolic redox chemistry⚡by recombining pre-existing energy-coupling modules into one integrated machine ⚙️
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
6/ Through subtomogram averaging, we found that an electron-transferring flavoprotein (ETF) reversibly associates with BCRII, identifying it as the physiological high-potential acceptor. ETF likely delivers electrons to menaquinone via EMO, linking aromatic degradation to the respiratory chain
Figure summarizing identification of ETF as the high-potential acceptor of BCRII. Left, a subtomogram average of the BCRII complex with extra density above BamD and a zoomed fitted model showing ETF bound at the BamD region. Right, schematic of the proposed electron-transfer pathway: electrons from reduced ferredoxin and NADH enter BCRII, are split into low- and high-potential branches, the low-potential branch drives aromatic ring reduction at the tungsten active site, and the high-potential branch is transferred to ETF. ETF then likely shuttles electrons to the membrane enzyme EMO, which reduces menaquinone.
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
5/ But one key component was still missing: the high-potential acceptor 🤔🔍 Earlier studies proposed that BCRII is membrane-attached and transfers electrons to menaquinone Using in situ #cryoET, we instead found BCRII dispersed throughout the cytoplasm, pointing to a soluble high-potential acceptor
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
4/ One striking feature of BamD, homologous to heterodisulfide-reducing subunits of methanogenic complexes, is the replacement of the distal canonical non-cubane cluster with a novel [3Fe–4S] cluster with a terminal sulfur ligand, reflecting reduction of a distinct high-potential acceptor
BamD region in BCRII. The center shows BamD as a green ribbon with multiple Fe–S clusters, adjacent to BamE in pink. Insets on the left and right compare the two distal non-cubane clusters: a canonical non-cubane [4Fe–4S] cluster on the left and the unusual modified non-cubane [3Fe–4S] cluster in BamD on the right.
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
3/ Mechanistically, electrons from NADH and reduced ferredoxin are confurcated at the HydBC-like module and then transferred to the FAD in the HdrABC-like module, where flavin-based electron bifurcation couples an exergonic branch to the endergonic reduction of the aromatic ring
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
2/ Using BCRII from Geobacter metallireducens as our model system, our cryo-EM structures show that the complex is built from three linked modules 🧩 known from electron-bifurcating hydrogenases, methanogenic heterodisulfide reductases and aldehyde oxidoreductases, respectively
Overview of the modular BCRII complex. The figure shows the full dimeric assembly and highlights its three main parts: the BamGHI electron-input/confurcation module, the BamDEF electron-bifurcation module, and the Bam(BC)2 catalytic module where aromatic ring reduction occurs. A simplified pathway diagram traces electron flow through the complex.
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Tomas Pascoa @tomaspascoa.bsky.social · 14/04/2026
1/ Excited to share our preprint! 🥳 Degradation of aromatic compounds, including BTEX pollutants, requires highly endergonic aromatic ring reduction. Using #cryoEM and in situ #cryoET, we show how BCRII couples electron bifurcation modules in one giant redox machine www.biorxiv.org/content/10.6...
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Caitie McCafferty @computingcaitie.bsky.social · 08/04/2026
I am excited to share our most recent work collaborating with @centriolelab.bsky.social and @stearnslab.bsky.social to look at the ciliary base of mammalian multiciliated cells w/ cryo-ET, XL/MS, and U-ExM www.biorxiv.org/content/10.6...
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Jan-Hannes Schaefer @jhschaef.bsky.social · 07/04/2026
We identified the maltoside detergent DM as an effective and easy solution to address preferred orientation in cryo-EM. Helped me switch from graphene grids. Special congrats to Maria Rafiq! @landerlab.bsky.social @nanigrotjahn.bsky.social @wisemanlab.bsky.social #cryoEM doi.org/10.64898/202...
Blender Rendering of vitrified HA trimer with DM at the air-water interface
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Sjors Scheres @sjorsscheres.bsky.social · 02/04/2026
Our latest @biorxivpreprint.bsky.social: "Prion-like transmission of human tau strains in the mouse brain" 🥳 With Michel Goedert and Masato Hasegawa. www.biorxiv.org/content/10.6...
biorxiv.org
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Alisia Fadini @alisiafadini.bsky.social · 01/04/2026
ROCKET 🚀 inference-time optimization of AlphaFold to fit structural data is published! rdcu.be/fa9YH Since our preprint, we’ve pushed it to regimes where other methods break: low resolution, weak signal, real experimental edge cases. Here’s what we learned: 1/15
rdcu.be
AlphaFold as a prior: experimental structure determination conditioned on a pretrained neural network
Nature Methods - ROCKET improves experimental structure elucidation by integrating implicit structural knowledge from OpenFold, a trainable reimplementation of AlphaFold2, with X-ray...
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Philippe Van der Stappen @phaips.vd.st · 20/03/2026
#TeamTomo if you want to use CTF-corrected 3D subtomos from AreTomo3 in RELION v.5.1 you can use this updated script: github.com/Phaips/aretomo3torelion5
github.com
GitHub - Phaips/aretomo3torelion5
Contribute to Phaips/aretomo3torelion5 development by creating an account on GitHub.
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Ricardo D. Righetto @lifeonthewedge.bsky.social · 19/03/2026
Meet Stoic from @daniil-litvinov.bsky.social and @ninjani.bsky.social: embeddings to predict stoichiometry of protein complexes from sequence fast and accurately 🧬🧩💻🤩 www.biorxiv.org/content/10.6...
Stoic:  Fast and accurate protein stoichiometry prediction (preprint header with authors and affiliations)
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Manon Demulder @manondemulder.bsky.social · 11/03/2026
Excited to announce I’m starting a new lab at @gmivienna.bsky.social (Vienna BioCentre) in Sept 2026 We study how carbon fixation is inherited and maintained in algae using cryo-ET, imaging, environmental sampling&more Looking for people who want to build the lab together, get in touch! #teamtomo
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John Rubinstein @johnrubinstein.bsky.social · 06/03/2026
I've written a review on what I think is an extremely exciting direction in cryo-EM: Cryo-EM of endogenous membrane proteins in their native lipid bilayer Open access in Quarterly Reviews of Biophysics: doi.org/10.1017/S003...
Figure 1. Cryo-EM of abundant protein complexes in native membranes.Figure 2. Cryo-EM of membrane proteins in vesicles.Figure 3. 3D reconstruction of V-ATPase in native synaptic vesicle membranes.Figure 4. Generation of membrane vesicles for structure determination of proteins in their native lipid bilayer.
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Florent Waltz @florentwaltz.bsky.social · 10/02/2026
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 🧵
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Ricardo D. Righetto @lifeonthewedge.bsky.social · 30/01/2026
Check out this cool thread on the latest preprint by Gaurav Kumar, @james-r-barrett.bsky.social, @phaips.vd.st from our lab and colleagues, dissecting the physics of Rubisco condensates! You're in for some stunning #cryoET of the pyrenoid - in Chlamy, of course 😉 Congrats to all involved!
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Juan Carlos De la Concepcion @delaconcepcionjc.bsky.social · 30/01/2026
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...
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Wilfling Lab @wilflinglab.bsky.social · 20/01/2026
LLOMe has long been used to study lysosomal damage, yet how it works has remained a mystery. Using cryo-electron tomography, we show it forms amyloid structures inside lysosomes that mechanically rupture membranes – revealing a new paradigm for lysosomal failure. 🔗 doi.org/10.64898/202... #CryoET
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Florent Waltz @florentwaltz.bsky.social · 19/12/2025
Final version is out! Our large-scale cryo-ET dataset 🔬 of Chlamydomonas reinhardtii 🦠 is now published in @cp-molcell.bsky.social Huge collaborative effort! So glad to see the community already using it to develop new resources & tools. Check it out here: shorturl.at/z4i4c #CryoEM #CryoET
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Allegretti Lab @matteoall.bsky.social · 19/12/2025
We are thrilled to share our new pre-print on the molecular anatomy of nuclear proteasome in human sperm cells! #In-cellcryo-ET + #SPA + #LM! @piotrkolata.bsky.social @a-dsantos.bsky.social, @tomdendooven.bsky.social!! doi.org/10.64898/202...
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bioRxiv Cell Biology @biorxiv-cellbio.bsky.social · 11/12/2025
IsoNet2 determines cellular structures at submolecular resolution without averaging www.biorxiv.org/content/10.64898/20…
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Ben Engel @cellarchlab.com · 10/12/2025
Happy to share our fun team-up with @centriolelab.bsky.social & @stearnslab.bsky.social to reveal the architecture of the mammalian centriole’s Distal Ring 🛟. Very cool multiscale integration of #UExM 📏🔬with #CryoET ❄️🔬. Congrats to @ebertiaux.bsky.social & @computingcaitie.bsky.social #TeamTomo 🧪
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Ariane Briegel @arianebriegel.bsky.social · 01/12/2025
CryoET of microbes inside an animal organ? Yes it’s possible! Check out our new preprint showing how we did it! What an amazing collaboration with amazing scientists who made this possible!
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Danielle Grotjahn @nanigrotjahn.bsky.social · 17/11/2025
Prohibitins aren’t hanging out just anywhere in the membrane — they prefer the 💁‍♀️💎✨VIP section💅🪩🥂 Lab all-star @mmedina300kv.bsky.social maps these microdomains using cryo-ET + surface morphometrics. s/o to #teamtomo #cryoET co-authors @hamid13r.bsky.social @attychang.bsky.social @baradlab.com
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Ricardo D. Righetto @lifeonthewedge.bsky.social · 23/10/2025
Our colleagues Vinith Kishore and Valentin Debarnot from the @ivandokmanic.bsky.social lab have come up with an amazing deep learning tool for denoising and filling the missing wedge in #cryoET data. I'm pleased to introduce Icecream🍧
biorxiv.org
Icecream: High-Fidelity Equivariant Cryo-Electron Tomography
Cryo-electron tomography (cryo-ET) visualizes 3D cellular architecture in near-native states. Recent deep-learning methods (CryoCARE, IsoNet, DeepDeWedge, CryoLithe) improve denoising and artifact cor...
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Ben Engel @cellarchlab.com · 23/10/2025
Hey #TeamTomo …would you like to try some 🍦ICECREAM!? Our @unibas.ch colleagues over at the @ivandokmanic.bsky.social lab have developed a stunningly effective tool to de-noise and de-wedge your tomograms. The contrast and details will give you brain freeze! 🍨❄️🤯 Please try, we need feedback 🧪🧶🧬🔬
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Jakob Meier-Credo @meiercredo.bsky.social · 19/09/2025
Check out our new preprint on an integrated pipeline combining in situ #cryo-ET with MALDI #MSImaging for single-cell identification and classification from previously analysed EM-grids. Link: www.biorxiv.org/content/10.1...
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Jan-Hannes Schaefer @jhschaef.bsky.social · 05/10/2025
Helical Reconstruction of Amyloids in cryoSPARC? We present guidelines, limitations & future perspectives for processing amyloids in cryoSPARC @structurabio.bsky.social. Great collaboration of the Kelly Lab and @landerlab.bsky.social #cryoEM #amyloid www.biorxiv.org/content/10.1...
Amyloid reconstructions from cryoSPARC
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