Claudio Alfieri

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

An integrated workflow for structural virology with a 100 keV electron microscope www.biorxiv.org/content/10.64898/2025.12.08.693081v1 #cryoEM

Our lab @mrclmb.bsky.social in Cambridge is seeking a passionate PhD student to explore transcription-coupled splicing! Join our team for an exciting project to understand human gene regulation 🧬 Feel free to get in touch directly #PhD #cryoEM #biochemistry

www2.mrc-lmb.cam.ac.uk/students/int...

Chris Russo and Anastasiia Gusach have developed a new method to prepare #cryoEM samples that avoids protein damage during freezing

Read more: www2.mrc-lmb.cam.ac.uk/a-new-method...

#LMBResearch

Interactions with the nucleosome’s acidic patch and DNA entry/exit site give the chromosomal passenger complex CPC a non-catalytic role in stabilizing #centromeric chromatin
#cryoEM and biochemical, cellular data by AA Jeyaprakash and coworkers
www.embopress.org/doi/full/10....

`Mix-it-up': accessible time-resolved cryo-EM on the millisecond timescale pubmed.ncbi.nlm.nih.gov/41140236/ #cryoEM

EMBL scientists have new detailed info about Asgard archaea DNA structures offering important clues to more complex cell evolution.

With #cryoEM, scientists found both open and closed chomatin structures with a possible role in regulating chromatin.

doi.org/10.1016/j.mo...

Structural dissection of αβ-tubulin heterodimer assembly and disassembly by human tubulin-specific chaperones pubmed.ncbi.nlm.nih.gov/41166473/ #cryoEM

On a gruelling hunt for rare associated molecules in your #cryoEM particle stack and not sure where to look?

Discover practical tips and tricks in our new case study using #CryoSPARC v4.7.1 where we find and refine a low-population interaction partner!

guide.cryosparc.com/processing-d...

Structural insights into cobalamin loading and reactivation of human methionine synthase Human methionine synthase (MTR) is an essential enzyme of one carbon metabolism. Consisting of a catalytic N-half and a cobalamin binding C-half, MTR utilises this intricate organometallic cofactor in...

I am excited to share our new preprint on our structural and biochemical analyses of human methionine synthase (MTR). This was the hard work of Douglas Ferreira who carried out this research as a significant part of his PhD. #CryoEM www.biorxiv.org/content/10.1...

Amazing work from my neighbour's lab! Many congrats to all the people involved! 👏👏👏👏

Part of something that we have been working on for a while-A 3.1 Å map of a flexibly tethered 38 kDa domain. Hopefully preprinted soon along with a few other structures. #CryoEM

This is super cool and great investigative work! Thanks Oli and co! #smallparticles #cryoEM

High-throughput investigation of cyclin docking interactions reveals the complexity of motif binding determinants - Nature Communications Many protein–protein interactions depend on Short Linear Motifs (SLiMs). In this study, the authors use large-scale binding assays, deep mutational scanning, and structural analysis to map SLiMs recog...

Just published: Our paper on high-throughput analysis of cyclin docking interactions, led by the group of Norman Davey @icr.ac.uk and with some small-complex-plus-peptide #cryoEM by @natalia-mg.bsky.social from my lab. Congratulations, everyone!
www.nature.com/articles/s41...

We’ve uncovered Asgard chromatin structures formed by a Hodarchaeal histone : closed hypernucleosome conserved in archaea and an open form resembling the H3-H4 eukaryotic octasome. Fantastic work by @harshranawat.bsky.social!
www.biorxiv.org/content/10.1...
#Chromatin #Asgard #Archaea #cryoEM

Our integrative approach using #MD and #cryoEM data to construct structural ensembles of #RNA just published on @natcomms.bsky.social doi.org/10.1038/s414... Lead by Elisa Posani, with @magistratolab.bsky.social @bonomimax.bsky.social @pjanos.bsky.social @navtejtoor.bsky.social and Daniel Haack 🎉

A snapshot of the HLp tetramer (purple) wrapping ~60 bp of DNA (green).

Excited to share our new preprint on HLp—a bacterial histone from Leptospira perolatii that forms stable tetramers and wraps ~60 bp of DNA: "DNA Wrapping by a Tetrameric Bacterial Histone" www.biorxiv.org/content/10.1...

@mpi-bio-fml.bsky.social

Many Congrats Sebastian and Team! 🥳🥳🥳

Determining the effects of pseudouridine incorporation on human tRNAs | The EMBO Journal imageimagetRNAs harbour a complex set of modifications which are important for their function. Here, single particle cryo-EM, biophysics, and computational analyses of the effects of pseudouridine inc...

We are very excited about our latest work, which just came out @embojournal.org – www.embopress.org/doi/full/10..... The work @MCB_UJ was driven by Anna Biela and Ting-Yu Lin 林亭妤 in collaboration with @jmbujnicki.bsky.social…a short🧵

New preprint on 3D heterochromatin architecture in human cells! Great collab with @sergiocruzleon.bsky.social & @johannesbetz.bsky.social from @hummerlab.bsky.social, @marinalusic.bsky.social & the Turoňová lab. Many thanks to my supervisor @becklab.bsky.social. bioRxiv: tinyurl.com/3a74uanv 🧵👇

#CryoSPARC v4.7 is out! 🚀 
Featuring a new automatic Micrograph Junk Detector that labels and rejects contaminants, new tools for curating subsets of particles, performance and stability fixes, and more!
Full changelog: cryosparc.com/updates

#cryoEM

🚨New paper🚨Our new study with the lab of Phil Cole uncovers how SIRT6 dynamically adapts structurally and enzymatically to target diverse histone acylations (e.g., H3K27ac) within nucleosomes. @jonmarkert.bsky.social
doi.org/10.1016/j.jb... #Chromatin #SIRT6 #CryoEM

Excited to share our new preprint on co-transcriptional splicing! U1 snRNP is recruited to RNA polymerase II through multiple interaction sites, with elongation factor SPT6 binding directly to the U1 snRNP protein.

www.biorxiv.org/content/10.1...

#cryoEM #transcription #splicing

Many congratulation Suyang and coauthors!

Structural basis for transcription activation through cooperative recruitment of MntR - Nature Communications MntR is a protein that can repress the expression of Mn2+ uptake transporters and activate the expression of efflux proteins. Here, the authors use cryo-EM and other biochemical approaches to establis...

How does MntR function as both repressor and activator with different Mn(II) sensitivity and cooperativity?

Led by the remarkable Prof. Shivani Ahuju (Reed), our long-time collaborator Arthur Glasfeld, and Reed undergraduates!
#MicroSky #ChemSky #cryoEM

www.nature.com/articles/s41...

Sad to know about the passing of Béla Novák. This review from Tyson, Chen and Novak was such a revelation for me as an introduction to control theory in biological systems. A classic that will remain relevant for many years to come. www.sciencedirect.com/science/arti...

📢 We’re looking for a new Team Leader!

@enasequence.bsky.social is recruiting a Team Leader to shape the strategy and direction for the ENA and Biosamples open data resources.

Interested?👇

Today in @nature.com we share our back-to-back stories with Ning Zheng’s lab revealing chemical-genetic convergence between a molecular glue degrader & E3 ligase cancer mutations. 1/5

Making intrabodies from antibodies just got easier! Learn how we made 𝟭𝟵 intrabodies to bind and light up peptides and histone modifications in live cells. And thanks to Academia, all sequences are freely available. (video credit: Yuko Sato @YukoSatoT2) (1/15)
www.biorxiv.org/content/10.1...

The mechanics of a continuous self-assembling surface-layer aids cell division in an archaeon

Tight collaboration with @buzzbaum.bsky.social, Sulfolobus cryo-ET from @idocaspy.bsky.social

www.biorxiv.org/content/10.1...