Matthew Clark
@matthew-batisio.bsky.social
1.2K followers 750 following 15 posts
Cellular Structural Biology Wellcome DPhil Student at The University of Oxford. Currently working in Peijun Zhang’s lab at The Oxford Division of Structural Biology. Passionate about biomedical animation and science communication: Batisio.co.uk
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matthew-batisio.bsky.social
I am excited to share this animation of the budding yeast inner kinetochore. Created for David Barford's lab @mrclmb.bsky.social

This DNA-binding protein complex acts as an anchor for the spindles that pull chromosomes apart during mitosis.
www.science.org/doi/10.1126/...

#blender #animation #b3d
Reposted by Matthew Clark
dyneinassembly.bsky.social
Happy to share the inaugural paper from the lab. We describe a molecular mechanism for the activation of outer dynein arm motors that power the vital motion of cilia.

Open access link below:
www.nature.com/articles/s41...

Here's a cool animated summary
Reposted by Matthew Clark
lapassmore.bsky.social
We have an open post-doc position in my group to study mRNA cleavage and polyadenylation using biochemical reconstitution and cryoEM.

Please get in touch if you are interested in joining this amazing team! 🔬🧬🤩
#RNA #cryoEM
Reposted by Matthew Clark
matthiaswilmanns.bsky.social
We are excited to share our latest work, where we unravel the structural and functional secrets of the once-mysterious protein Pex8 revealing how it controls the peroxisomal cargo import receptor Pex5.

Read more here: www.biorxiv.org/content/10.1101/2025.08.30.673231v1
Ensemble model of the full length Pex5 receptor (different blue color) in complex with Pex8 (green colors).

Key Findings:

Pex8 binds to a novel site on the mostly unfolded N-terminal region of the Pex5 receptor. This interaction is essential for peroxisomal protein import.

Computational modelling reveals the formation of an assembly with the trimeric peroxisomal E3-ubiquitin ligase.

We propose that this action positions the Pex5 receptor for its recycling, a step essential for the entire protein import process.

Why this matters:

Peroxisomes rely entirely on the import of folded proteins to function. Impaired peroxisome function is linked to severe disorders, and recent data show their crucial roles in carcinogenesis and the immune response. Our work elevates Pex8 from an enigma to a central player in this critical biological process.

Read the full story and see the structures here: https://www.biorxiv.org/content/10.1101/2025.08.30.673231v1

#CellBiology #StructuralBiology #Peroxisome #ProteinImport #bioRxiv #Biochemistry
Reposted by Matthew Clark
amunts.bsky.social
Stunning cryo-ET from Peijun Zhang lab: Direct visualization of HIV-1 nuclear import!
Hundreds of viral cores captured entering the nucleus. The NPC dilates to let the capsid through. A masterclass in correlative microscopy that makes it quantitative. A leap for structural virology! @emboreports.org
Reposted by Matthew Clark
martinpacesa.bsky.social
Exciting to see our protein binder design pipeline BindCraft published in its final form in @Nature ! This has been an amazing collaborative effort with Lennart, Christian, @sokrypton.org, Bruno and many other amazing lab members and collaborators.

www.nature.com/articles/s41...
Reposted by Matthew Clark
gautamdey.bsky.social
Want to acquire #ExM images like this and help us understand the true extent of cytoskeletal diversity across the tree of life? This position might be for you!

embl.wd103.myworkdayjobs.com/en-US/EMBL/j...

With @dudinlab.bsky.social
@embl.org @biology-unige.bsky.social @moorefound.bsky.social
Reposted by Matthew Clark
watchclockwork.com
🕒 NEW VIDEO 🕒

How can a cell know the time? Let's explore the beautiful 24-hour cycle produced by #KaiC proteins in the cyanobacteria S. Elongatus. Rendered in #blender3d with @bradyajohnston.bsky.social's brilliant Molecular Nodes add-on. #biology
matthew-batisio.bsky.social
Awesome video! I love how you represented the slow C1 domain hydrolysis.
Reposted by Matthew Clark
rezamehdipour.bsky.social
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...
Reposted by Matthew Clark
carter-lab.bsky.social
Excited to share our latest work with @simonbullock11.bsky.social! We looked at how diverse mRNAs get selected for subcellular localization and it turns out that a single protein can recognize different RNA elements using shared features that weren’t apparent before.
www.biorxiv.org/content/10.1...
Reposted by Matthew Clark
jordanraff.bsky.social
The Dunn School is a really great environment for taking up a Career Development Fellowship, and we are looking for candidates! Please spread the word.
dunnschool.bsky.social
📣 Applications now open 📣

We are seeking outstanding ECRs looking for a stimulating and supportive environment in which to establish their research group as externally-funded fellows, in any area or cell or molecular biology underlying disease!

Please share!

www.path.ox.ac.uk/work-with-us...
Reposted by Matthew Clark
dr-downes.bsky.social
Very excited to announce that my first, first author paper, is now on BioRxiv! In this paper we unambiguously show #COPII coated vesicles in unperturbed human cells for the very first time!!

Make my day and check it out!
www.biorxiv.org/content/10.1...

#Cryo-ET #TeamTomo #Cryo-CLEM ❄️🔬❄️🔬❄️🔬❄️🔬
Reposted by Matthew Clark
kattoropova.bsky.social
Thrilled to see our study on how kinesin-2 motors are switched on and off published in @natsmb.nature.com ⚛️

➡️ www.nature.com/articles/s41...

Congrats to all authors from me and Anthony 🎉 @dunnschool.bsky.social Check out this animation made by talented PhD student @matthew-batisio.bsky.social 😆
Reposted by Matthew Clark
costalaboratory.bsky.social
Less than two weeks left to apply!

Postdoc positions in my lab to study

1. initiation of DNA replication.

2. chromatin replication/epigenetic inheritance.

Great for biochemists, biophysicists & structural biologists.

Deadline 3 August 2025.

crick.wd3.myworkdayjobs.com/External/job...
Postdoctoral Fellow - Costa Lab
Salary for this Role: From £45,500 with benefits, subject to skills and experience. Job Title: Postdoctoral Fellow - Costa Lab Reports to: Alessandro Costa Closing Date: 03/Aug/2025 23.59 GMT Job Desc...
crick.wd3.myworkdayjobs.com
matthew-batisio.bsky.social
Awesome work, and a beautiful graphical abstract!
Reposted by Matthew Clark
parasitematt.bsky.social
Delighted to share the final version of Richard Zhou's study on how the CD163 scavenger receptor cleans up after toxic haemoglobin spills out from our blood cells. An amazing grabber mechanism!
rdcu.be/ewPA2
Reposted by Matthew Clark
dannybhgold.bsky.social
🎉 Excited to share my first paper as 2nd author! From the Barr & Gruneberg labs, this work explores the structure of the Chromosome Passenger Complex (CPC) and suggests a ‘pivot–tether’ model for how it binds H3pT3-phosphorylated nucleosomes
@oxfordbiochemistry.bsky.social @dunnschool.bsky.social
matthew-batisio.bsky.social
IFT trains are really cool - and what better way to communicate their structure than baking a cake?

Created for my 1st year PhD project with Anthony Roberts and @kattoropova.bsky.social

IFT-A 🟡 IFT-B 🟢 Dynein-2 🔵
Matthew Clark holding a tray with a layered rectangular cake, showing the periodic repeating structure of IFT-A and IFT-B. Gingerbread cookies cut in the shape of dynein-2 ride on top. A close up photo of the cake on a table, showing the periodic repeating structure of IFT-A and IFT-B. Gingerbread cookies cut in the shape of dynein-2 ride on top.
Reposted by Matthew Clark
stanislauy.bsky.social
Happy to share our latest work on the structure and assembly of holocentric kinetochores! Huge thanks to Ines for a very fruitful collaboration, Claudio for all the support, and congratulations to Christine and all co-authors!

www.biorxiv.org/content/10.1...
Reposted by Matthew Clark
ccemmp-outreach.bsky.social
Big news! 📢CCeMMP is holding the 2nd 'Bench to Art' Exhibition to showcase the artistic flair of structural biology. Share your creations to be displayed in a virtual gallery during National Science Week & for a chance to win cash prizes 💰! More info: ccemmp.org/events/arc-c...

#CryoEM
#Membranes
Reposted by Matthew Clark
jlsteenwyk.bsky.social
NEW pub: The role of metabolism in shaping #enzyme structures over 400 million years. Now out in @nature.com

Super grateful to have played a small role in this project - congrats to lead/corr authors Oliver, Benjamin, and Markus!

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

#alphafold #evolution #genomics
Reposted by Matthew Clark
suyangzhang.bsky.social
Excited to share our latest work! We found transcription factor SPT6 and phosphorylated Pol II CTD help recruit U1 snRNP to elongating Pol II, allowing efficient co-transcriptional splicing.

Glad to be featured in the Editors’ Highlights!

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

#splicing #cryoEM
Reposted by Matthew Clark