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
😳

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! 🤗

Mother Nature is still the undisputed Queen of organic chemistry!

Figure 4 from the preprint

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...

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...

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

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!🎉

7/ Together, this work shows how evolution can expand metabolic redox chemistry⚡by recombining pre-existing energy-coupling modules into one integrated machine ⚙️

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.

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

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

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.

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

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

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.

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

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...

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...

Blender Rendering of vitrified HA trimer with DM at the air-water interface

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...

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...

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...

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

#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

Stoic: Fast and accurate protein stoichiometry prediction (preprint header with authors and affiliations)

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...

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

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.

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...

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 🧵

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!

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...

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

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

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...

IsoNet2 determines cellular structures at submolecular resolution without averaging www.biorxiv.org/content/10.64898/2025.12...

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 🧪