Out at Nat Commun: Stereoselectivity and plasticity of a common binding pocket in TRPM3 One pocket, many ligands. CryoEM & electrophysiology reveal a promiscuous site where mutations rewire stereoselectivity and invert the functional outcome of ligand binding nature.com/articles/s41467-026-71226-0

Game changer, no doubt. Commercial systems will have expensive consumables I suppose, but huge savings to be made in cell culture, and many important but sparse native targets come into play. Crispr-tagged targets from iPSC neurons, for example. TRPC6 blind? 🤯

Janine Brunner@janinebrunner.bsky.social · 9mo ago

MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Or from a single dish of HEK cell culture in the case of two membrane proteins. Out in Nature Methods now! lnkd.in/gpyBSceg Wonderful collaboration with the Efremov lab.

MISO: microfluidic protein isolation enables single-particle cryo-EM structure determination from a single cell colony. Or from a single dish of HEK cell culture in the case of two membrane proteins. Out in Nature Methods now! lnkd.in/gpyBSceg Wonderful collaboration with the Efremov lab.

New lab preprint! @zestytoast.bsky.social tagged a scarce mycobacterial protein in M. smegmatis with TwinStep but got… something? @kjamali.bsky.social's ModelAngelo built models & @martinsteinegger.bsky.social's FoldSeek IDed them as the biotin-containing MCC & LCC complexes 🧵 tinyurl.com/ukny4ptz

Please RT. Post-doc opportunity alert! 💥 closing 10th December.. Come join our team (www.thelowlab.org) at Imperial, London, working on the structure and mechanism of bacterial secretion systems. For more details and to apply please see www.imperial.ac.uk/jobs/search-...

Happy to announce our most recent preprint: Stereoselectivity and plasticity of a common binding pocket in TRPM3, by cryo-EM and elecrophysiology. Great collaboration with the Voets, Vriens and CISTIM labs. www.biorxiv.org/content/10.1...

Happy to share the latest from the lab, led by Daniel Alvarez, in collaboration with @lizconibear.bsky.social‬. In this AA-MD tour-de-force, we delve deep into the mechanism and energetics of lipid uptake by bridge-like lipid transfer proteins, and we learn a few interesting things along the way...

bioRxiv Biophysics@biorxiv-biophys.bsky.social · last yr.

The molecular mechanism of lipid uptake by membrane-anchored bridge-like lipid transfer proteins. https://www.biorxiv.org/content/10.1101/2025.08.01.668188v1

We are excited to announce the first in-cell structure of a LINC complex within a native nuclear envelope at subnanometer resolution!! #In-cell cryo-ET + #atomistic MD simulations! @tomdendooven.bsky.social et al!! www.biorxiv.org/content/10.1...

Happy to share the latest work from the lab, led by @mudgal17.bsky.social‬, in collaboration with the Weis lab @ethzurich.bsky.social. How do nuclear membranes fuse during NPC assembly? We answer this question in our latest work, where we identify a new mechanism for membrane fusion… (1/13)

bioRxiv Cell Biology@biorxiv-cellbio.bsky.social · last yr.

A conserved mechanism of membrane fusion in nuclear pore complex assembly https://www.biorxiv.org/content/10.1101/2025.07.21.665908v1

New preprint in the lab combining what we like best: insects, love, chemistry and the olfactory system! 1/8 www.biorxiv.org/content/10.1...

A covalent recognition strategy enables conspecific mate identification

The olfactory system can detect an uncountable number of volatile molecules while retaining the ability to discriminate amongst very similar ones. We identified a unique mechanism employed by insect o...

biorxiv.org

Excited to share our latest story in Nature. We developed a high-throughput cellular stretch system to look for genes regulating membrane rupture under tension, and found an amazing small protein called NINJ1 that weakens the membrane for rupture! H/T to Zozo, my 10-y.o. for her artist's impression😃

Check out this remarkable debut paper from @jie-xu.bsky.social, a very creative lab alumnus. Very proud! www.nature.com/articles/s41...

Jie Xu@jie-xu.bsky.social · last yr.

Excited to share our latest story in Nature. We developed a high-throughput cellular stretch system to look for genes regulating membrane rupture under tension, and found an amazing small protein called NINJ1 that weakens the membrane for rupture! H/T to Zozo, my 10-y.o. for her artist's impression😃

I’m thrilled to finally share this preprint! It contains a WOW Cryo-EM structure (likely one of the strongest protein fibers known to man 🤯), but we’ve also untangled its biological function: a novel type of virulence factor💀! www.researchsquare.com/article/rs-6...

@mikesleutel.bsky.social · last yr.

In our latest preprint we used cryoEM to solve the structure of A-ENA fibers and show that they are stabilized by 10 isopeptide bonds per monomer. A-ENA couples the spore to the cry-toxins, and in doing so increases the virulence of Bacillus thuringiensis: www.researchsquare.com/article/rs-6...

In our latest preprint we used cryoEM to solve the structure of A-ENA fibers and show that they are stabilized by 10 isopeptide bonds per monomer. A-ENA couples the spore to the cry-toxins, and in doing so increases the virulence of Bacillus thuringiensis: www.researchsquare.com/article/rs-6...

I am delighted to share our findings on the binding mode of tetanus neurotoxin and the anti-epileptic drug Levetiracetam to SV2A, an essential synaptic vesicle membrane protein of unknown function, now online in @NatComms.bsky.social   www.nature.com/articles/s41...

Structures of native SV2A reveal the binding mode for tetanus neurotoxin and anti-epileptic racetams - Nature Communications

SV2A, an essential membrane protein in neurotransmission, is known as the receptor of clostridial neurotoxins and target of anti-epileptic drugs. Here the authors show details of the binding site for ...

nature.com

Please RT. Post-doc opportunity alert! 💥 Come join our team (thelowlab.org) at Imperial, London, working on bacterial secretion systems. The position is funded by the Wellcome Trust. For more details and to apply please see www.imperial.ac.uk/jobs/search-...

Here's our newest study: we reveal the molecular principles of neuronal excitation by glutamate, and how physiological temperatures influence this process. www.nature.com/articles/s41... www.nature.com/articles/d41... Led by @anish-mondal07.bsky.social, published in @natureportfolio.nature.com

Structural basis of ClC-3 inhibition by TMEM9 and PI(3,5)P ₂ pubmed.ncbi.nlm.nih.gov/40093093/ #cryoEM

Happy to share our latest publication on @naturesmb.bsky.social Natural Structure & Molecular Biology, we show tau filaments show Alzheimer fold in mutants V337M and R406W. thanks @sjorsscheres.bsky.social and Michel Goedert's support. 🥳 rdcu.be/edqzW rdcu.be/edoGv

Mutant tau filaments from some inherited frontotemporal dementias show the Alzheimer fold

Nature Structural & Molecular Biology - Frontotemporal dementias can be caused by mutations in MAPT, which encodes the protein tau; the mutant protein forms harmful aggregates in the brain....

rdcu.be

Thrilled to share the structure of dimerised human PINK1 docked to an endogenous translocase array on the mitochondrial surface, composed of two TOM complexes, bridged by a VDAC2 dimer! Published today in Science www.science.org/doi/10.1126/... @wehi-research.bsky.social @komanderlab.bsky.social

Themis and Grb2 form a constitutive structural hub in TCR signaling doi.org/10.1101/2025... @savvideslab.bsky.social

Just because it's a homo-oligomer, don't assume it's symmetric! @benjabsnt.bsky.social & collaborators used cryo-EM to study the transthyretin (TTR) tetramer (55 kDa), shedding light on its misfolding pathways linked to amyloid disease. Now in peer-reviewed form: www.nature.com/articles/s41...

In a great collaboration with @hummerlab.bsky.social and the Kräusslich lab: HIV capsid doesn't break at the NPC; instead, it cracks open the NPC itself! Details in Cell: authors.elsevier.com/sd/article/S... @mpibp.bsky.social @uniheidelberg.bsky.social A thread below:

Protein production for cryoEM structure determination just got a lot cheaper - high resolution structure from half a plate of HEK cells with the "MIcro ISolation (MISO)" microfluidics-based approach. Congrats to the Brunner and Efremov labs in Brussels! www.biorxiv.org/content/10.1...

Cryo-EM structures of mammalian membrane proteins from a single cell culture dish? Yes, Micro ISOlation (MISO) sample preparation makes it possible. www.biorxiv.org/content/10.1... Happy to be part of this exciting story and wonderful collaboration with the Rouslan Efremov lab.

Love this.. 👏 MISO: Microfluidic protein isolation enables single particle cryo-EM structure determination from a single cell colony www.biorxiv.org/content/10.1...