Guillaume Gaullier
eLifeHigh-resolution #CryoET provides ‘compelling’ evidence for the true 3D architecture of glutamatergic synapses: a complex ‘synaptoplasm’ rather than the textbook postsynaptic density.
https://elifesciences.org/articles/100335?utm_source=mastodon&utm_medium=social&utm_campaign=organic
A new #CryoET study shows that the protein ZapD helps organise FtsZ filaments into stable ring-like structures in building bacterial division machinery.
https://elifesciences.org/articles/95557?utm_source=mastodon&utm_medium=social&utm_campaign=organic
https://elifesciences.org/articles/95557?utm_source=mastodon&utm_medium=social&utm_campaign=organic
🌱 Using ‘compelling’ methods, including #CryoET, researchers mapped spinach thylakoid membranes at single-molecule precision, revealing how photosynthetic complexes are organised and settling long-standing debates on chloroplast architecture.
https://elifesciences.org/articles/105496?utm_source=mastodon&utm_medium=social&utm_campaign=organic_assessment
https://elifesciences.org/articles/105496?utm_source=mastodon&utm_medium=social&utm_campaign=organic_assessment
Pietro RoversiErice Structural Biology Course 2026 (29 May–6 Jun): apply! Train in Cryo-EM, Cryo-ET & ML to study macromolecular assemblies in cells. Hands-on + theory for next-gen structural cell biology.
🔗 erice2026.azuleon.org/application....
#CryoEM #CryoET #MachineLearning #StructuralBiology #CellBiology
International School of Crysta...
International School of Crysta...
SBGridMeharry Medical College Ph.D. candidate KeAndreya Morrison's highlight features a @Nature Structural & Molecular Biology publication from the lab of Chi-Min Ho of Columbia University and colleagues who used cryo-electron tomography to map malaria’s ribosomes at work and reveal how a parasite-specific drug derails translation.
Read more here: https://medium.com/sbgrid-community-news/stopping-ribosomes-in-action-101e95f41784
BenjaminHimesOne highlight from Friday that I forgot: Alister Burt's talk on his efforts to build #TeamTomo, a set of community-supported software packages and metadata standards for #cryoET. This is difficult work, and less rewarding for those in academia, but so essential. It's great to see progress on this front.
The other great news from Alister's talk: Warp is now supported on Linux!
Finally, I'll remember his advice "think about geometry, and use it if you can" when assigning initial particle orientations for subtomogram averaging.
preLightsAs we continue our #polaroidproject at #biologists100, we now feature Matteo Allegretti ✨
Matteo is presenting work on the macromolecular architecture of male germ nuclei - part of which can be found as a preprint on #bioRxiv
#preprint: https://www.biorxiv.org/content/10.1101/2024.10.30.620797v2
Human spermatogenesis leads to a reduced nuclear pore structure and function
Nuclear pore complexes (NPCs) are nuclear gateways which regulate the transit of molecules larger than 40kDa through a Ran-dependent transport[1][1]. The somatic human NPC scaffold consists of three stacked rings: the cytoplasmic (CR), the nucleoplasmic (NR), and the inner ring (IR), which define a central channel approximately 55nm wide[2][2]. Although many studies have investigated human NPC architecture[3][3], it remains largely unknown how the NPC accommodates the different functions of non-somatic cells. Here, we reveal the in-cell architecture of the human sperm NPC. We show that it exhibits a central channel less than 40nm-wide, outlined exclusively by the IR. This structural alteration is accompanied by a six-fold reduction in nuclear diffusion rate and mis-localization of Ran-dependent transport components. Additionally, we identify a network of septin filaments interconnecting NPCs within the inter-membrane space of the nuclear envelope (NE), suggesting a potential mechanical role in channel constriction. Furthermore, our human tissue imaging data indicate meiosis as a pivotal differentiation stage driving architectural changes to the NPC. Given the critical role of the IR for successful spermatogenesis[4][4],[5][5], our work offers important insight into this fundamental biological process. Our study also demonstrates the power of an integrative approach by combining electron-cryo- tomography, super-resolution-light-microscopy and biochemical analysis, to elucidate macromolecular structure-function relations in human physiological contexts. ### Competing Interest Statement The authors have declared no competing interest. [1]: #ref-1 [2]: #ref-2 [3]: #ref-3 [4]: #ref-4 [5]: #ref-5
Amelia Cervera 🧬In-cell structure and snapshots of copia retrotransposons in intact tissue by cryoelectron tomography
#Transposons #Retrotransposons #Ty1Copia #VLP #CryoET #Drosophila
https://www.cell.com/cell/fulltext/S0092-8674(25)00159-X
#Transposons #Retrotransposons #Ty1Copia #VLP #CryoET #Drosophila
https://www.cell.com/cell/fulltext/S0092-8674(25)00159-X