Well done. But is GTP-tubulin in an expanded state at the tip of growing microtubules? Indeed, nobody knows 🤔
Check the little video they made from the interview (with the “Rolex” Rave skateboards tee-shirt 😆)
I love us
We are very pleased to announce Prof. Paul Guichard and Dr. Virginie Hamel @centriolelab.bsky.social as joint winners of the RMS Award for Light Microscopy 🔬 👏 🏅
Huge congratulations to both!
Read more about Paul and Virginie's achievements: www.rms.org.uk/resource/pro...
The new release of #BigVolumeBrowser (0.1.0) finally adds animation render functionality to it, plus some other navigation improvements and bug fixes.
Here is a movie I've made for the microtubule network (via ExM) in different cell types. Contact me if you want it for educational/research purposes.
La #plateforme TEM2C de l'UAR Biosit propose ses services en cryo-microscopie électronique, cryo-tomographie et cryo-CLEM pour la biologie structurale et cellulaire ➡️ www.ibisa.net/plateformes-... @cnrsbiologie.bsky.social @inserm.fr @rennesuniv.bsky.social
Try this new online training game from Leandro F. Estrozi designed for newcomers in structural biology, with a focus on cryo-EM and cryo-ET map interpretation: rico.ibs.fr/helixplo...
Denis Chrétien
Christophe 🔬 Leterrier
Leah
Nice story 😎
So lovely 😍
Looks cool, will try!
Royal Microscopical Society
GIS IBiSA
Eugene Katrukha 🇺🇦
RCSB Protein Data Bank
Video
Denis Chrétien
Denis Chrétien
Denis Chrétien
I was interviewed by @snehakhedkar.bsky.social for The Scientist about our work using super-resolution microscopy to map the neuronal architecture, and make nice pictures along the way! Check the article here: www.the-scientist.com/super-resolu...
Approches intégrées de cryo-microscopie électronique, cryo-tomographie et cryo-CLEM pour la biologie structurale et cellulaire.
New preprint! In collaboration with the Steinmetz Lab at PSI we report cryo-EM structures of microtubules at up to 1.9 Å (!) resolution & in different nucleotide state mimics, suggesting a mechanism for lattice-induced GTP hydrolysis and why it leads to catastrophe: tinyurl.com/7cjrf863
Christophe 🔬 Leterrier
We're happy to announce our new preprint! 🐸 easymode: general pretrained networks for cellular cryo-ET. Segment ~20 cellular features – ribosomes, microtubules, mitochondria, nuclei & more – with zero model training. 🔗 doi.org/10.64898/202... 🧵👇
Wieczorek Lab
This deep sea creature is as sharp & clear as broken class, & can grow as long as your hand. This giant amphipod, (Cystisoma) only has two colored body parts: the dense orange stomach/egg pouch, & two MASSIVE eyes, which are a glittering holographic orange layer completely covering its head.
📽️ MBARI
Video
Glad to see the work of my PhD on the manchette microtubule now out in @embojournal.org: doi.org/10.1038/s443...
Microtubule comets in human iPSCs to kick off my first week of grad school! ☄️💫
Allegretti Lab
Video
Christophe Leterrier uses advanced microscopy to uncover neurons’ intricate nanostructure and dynamics while creating striking images that bring brain science to life.
The manchette is a transient microtubule (MT)-based structure that is vital for the correct shaping of sperm during spermiogenesis. Throughout spermiogenesis, the manchette retains structural integrity for several days, raising the question of how its MTs are regulated. Here, using cryo-electron tomography of manchettes isolated from rat testes, we find that manchette MT ends are structurally diverse. We show that the MT-binding protein CLASP2 is present throughout the manchette and likely regulates both MT ends. Using cryo-electron microscopy single particle analysis and super-resolution microscopy, we reveal that SPACA9 and MNMIP1 (SH3D21) bind to the seam of manchette MTs from the luminal side. SPACA9 binds to both α- and β-tubulin of protofilament 1 but does not interact directly with protofilament 13, while MNMIP1 binds directly to protofilament 13. MNMIP1 further extends and threads through the MT lattice at the seam. Our study reveals a novel seam MT inner protein complex with a unique binding mode, providing a plausible explanation for MT regulation that maintains manchette integrity over an extended period.