Reports of diverse stoichiometries have complicated our understanding of the complex between ALK kinase and its #cytokine ligand ALKAL2. @janfelix &co reanalyze #cryoEM data to clarify the situation @PLOSBiology https://plos.io/4lvRfvu
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Great to see Rebekka Wild's group going from strength to strength.
Structural basis for human chondroitin sulfate chain polymerization | bioRxiv
#StructuralBiology #CryoEM #Glycotime
#Science #Research
https://www.biorxiv.org/content/10.1101/2025.03.21.644485v1?rss=1
bioRxiv · Structural basis for human chondroitin sulfate chain polymerizationChondroitin sulfates are complex polysaccharide chains that regulate various biological processes at the cell surface and within the extracellular matrix. Here, we identify four heterodimeric complexes responsible for chondroitin sulfate chain polymerization in humans: CHSY1-CHPF, CHSY1-CHPF2, CHSY3-CHPF and CHSY3-CHPF2. Using a novel in vitro glycosylation assay based on chemo-enzymatically synthesized fluorescent substrates, we demonstrate that all four complexes exhibit chain polymerization activity. The cryo-EM structure of the CHSY3-CHPF complex provides, for the first time, molecular insights into the chondroitin sulfate chain polymerization reaction. The architecture of the catalytic sites suggests that CHSY1 and CHSY3 are enzymatically active, while CHPF and CHPF2 primarily play a stabilizing role. Mutational analysis of purified enzyme complexes, combined with an in cellulo complementation assay, confirms that only CHSY1 and CHSY3 have bifunctional glycosyltransferase activities. Based on the spatial arrangement of the catalytic sites, we propose that chondroitin sulfates chain polymerization follows a non-processive, disruptive mechanism.
### Competing Interest Statement
The authors have declared no competing interest.
Structural mechanism of LINE-1 target-primed reverse transcription.
#Transposons #Retrotransposons #LINE1 #ReverseTranscription #CryoEM
https://www.science.org/doi/10.1126/science.ads8412
Have you used one of the NIH sponsored #cryoEM centers and thought that was a great resource but looking to meet & interact with your peers? Ready to share and learn about other people’s experiences with using cryoEM?
Then join us at the #MM2025 Pre-Meeting Congress (PMCX61) on Transformative CryoEM in Salt Lake City, UT on Sunday, July 27, 2025.
Early registration deadline is May 8, 2025:
https://mmconference.microscopy.org/registration-information
Bacterial ABC peptide transporters are involved in processes like nutrient uptake. This study solves #cryoEM structures of the #Ecoli dipeptide #transporter DppABCDF in both apo & ATP analog-bound forms, providing insights into assembly & import mechanism #plosbiology https://plos.io/3DxP8pU
New preprint I contributed to: https://doi.org/10.1101/2025.02.17.638584
I helped this group do atomic model building and refinement in their #cryoEM maps.
This was more model building than I had done with all my previous projects combined! And it made me streamline the process I described in this thread: https://fediscience.org/@Guillawme/113281867808537736
#Bacterial #flagellar motors: Study sheds light on their #ion-driven mechanisms.
https://phys.org/news/2025-02-bacterial-flagellar-motors-ion-driven.html
phys.orgBacterial flagellar motors: Study sheds light on their ion-driven mechanismsWhen speaking of motors, most people think of those powering vehicles and human machinery. However, biological motors have existed for millions of years in microorganisms. Among these, many bacterial species have tail-like structures—called flagella—that spin around to propel themselves in fluids. These movements employ protein complexes known as the "flagellar motor."
CryoCrane, a visualization tool for cryo-EM screening data, aims to provide an intuitive way to visualize micrographs and to speed up data analysis. #CryoEM #SampleOptimization #GridScreening https://doi.org/10.1107/S2053230X25000081
The micrograph denoiser in CryoSPARC is really good! Fast training and denoising, excellent output (more helpful than topaz denoise; both run with their default settings).
Why didn't I start using it earlier??
Cryogenic Electron Microscopy: MagIC beads for scarce macromolecules. #CryoEm
https://elifesciences.org/articles/105335?utm_source=mastodon&utm_medium=social&utm_campaign=organic_insights
It's great to *finally* have both a direct work-related reason and enough free time these past two days to immerse myself in the two atomic resolution #cryoEM papers from 2020 and give them a good, thorough, cover-to-cover read. 
Feeling like it's an important step through the never-ending backlog of important papers in this field. 
Nakane et al. 2020: https://doi.org/10.1038/s41586-020-2829-0
Yip et al. 2020: https://doi.org/10.1038/s41586-020-2833-4
CryoCrane is a visualization tool for cryo-EM screening data that aims to provide an intuitive way to visualize micrographs and to speed up data analysis. #CryoEM #SampleOptimization #GridScreening https://doi.org/10.1107/S2053230X25000081
This is pretty amazing. TMEM206 structure determined using a single HEK cell colony!
"MISO: Microfluidic protein isolation enables single particle cryo-EM structure determination from a single cell colony”
bioRxiv · MISO: Microfluidic protein isolation enables single particle cryo-EM structure determination from a single cell colonySingle particle cryo-EM enables reconstructing near-atomic or even atomic resolution 3D maps of proteins by visualizing thousands to a few million purified protein particles embedded in nanometer-thick vitreous ice. This corresponds to picograms of purified protein, which can potentially be isolated from a few thousand cells. Hence, cryo-EM holds the potential of one of the most sensitive analytical methods that deliver a high-resolution protein structure as a readout. In practice, more than a million times more starting biological material is required to prepare cryo-EM grids. To close the gap, we developed a micro isolation (MISO) method that combines microfluidics-based protein purification with cryo-EM grid preparation. We validated the method on soluble bacterial and eukaryotic membrane proteins. We showed that MISO enables protein structure determination starting from below one microgram of a target protein and going from cells to cryo-EM grids within a few hours. This scales down the purification by a factor of a few hundred to a few thousand and opens possibilities for the structural characterization of hitherto inaccessible proteins.
### Competing Interest Statement
G.E. and R.G.E are inventors on the patent application WO WO2023/232662/A1 disclosing the MISO instrument and chip design filed by VIB and VUB.
Last days to apply!
We are recruiting #PhD 
students! We use functional #genomics and #StructuralBiology to study gene expression 
-> 
and we have open #PhDpositions!
The #PhDprogram application deadline is January 14, 2025.
#transcription #bioinformatics #cryoem #transcriptomics #ScienceMastodon #AcademicMastodon #PhDstudent #mpinat
Application link: https://uni-goettingen.de/de/application/556704.html
NEW - From us!
Capture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl https://www.nature.com/articles/s41594-024-01425-0
It's be a long and difficult birth, but it is finally out there. Lovely bit of integrative CryoEM revealing a crucial kinase/substrate complex in the determination of cell polarity - how cells know which way is up.
NatureCapture, mutual inhibition and release mechanism for aPKC–Par6 and its multisite polarity substrate Lgl - Nature Structural & Molecular BiologyCombining structural, biochemical, cellular and in vivo assays, the authors uncover the mechanism for capture and multisite phosphorylation of lethal (2) giant larvae by the atypical protein kinase C and partitioning-defective protein 6, revealing the basis for their mutual antagonism underpinning cell polarity.
Postdoctoral Scholar-Structural Biology in Protein Dynamics
Icahn School of Medicine at Mount Sinai
Join our lab as a #StructuralBiology #Postdoc to study proteins in #Alzheimers & #Cancer using #CryoEM & #XrayCrystallography at Mount Sinai!
See the full job description on jobRxiv: https://jobrxiv.org/job/icahn-school-of-medicine-at-mount-sinai...
https://jobrxiv.org/job/icahn-school-of-medicine-at-mount-sinai-27778-postdoctoral-scholar-structural-biology-in-protein-dynamics-2/?feed_id=89569
jobRxiv · Science Jobs - Find science and research jobsThe international job board for scientists, by scientists. Find science jobs in academia or industry: MSc, PhD, Postdoc, Scientist, Faculty and more!
Structural mechanism of CB1R binding to peripheral and biased inverse agonists | Nature Communications
Lovely bit of work. #CryoEM #Crystallography #Science #Research @strucbio
NatureStructural mechanism of CB1R binding to peripheral and biased inverse agonists - Nature CommunicationsPeripherally restricted CB1 inhibitors retain the weight loss benefits of this drug class while sparing the negative psychiatric side effects. The authors here elucidate cryo-EM structures of CB1 bound to peripherally restricted inhibitors to explain these drugs’ molecular mechanism of action.
Replied in thread
when blurred by the CTF (psf)Postdoctoral Scholar-Structural Biology in Protein Dynamics
Icahn School of Medicine at Mount Sinai
Join our lab as a #StructuralBiology #Postdoc to study proteins in #Alzheimers & #Cancer using #CryoEM & #XrayCrystallography at Mount Sinai!
See the full job description on jobRxiv: https://jobrxiv.org/job/icahn-school-of-medicine-at-mount-sinai...
https://jobrxiv.org/job/icahn-school-of-medicine-at-mount-sinai-27778-postdoctoral-scholar-structural-biology-in-protein-dynamics-2/?feed_id=89072
jobRxiv · Science Jobs - Find science and research jobsThe international job board for scientists, by scientists. Find science jobs in academia or industry: MSc, PhD, Postdoc, Scientist, Faculty and more!
Structure and assembly of the dystrophin glycoprotein complex | Nature
Bit of a beast. Used to work on the matriglycan modification of aDG, nice to see this out in the wild.
#CryoEM #Science #Research #MuscularDystrophy #StructuralBiology @strucbio
NatureStructure and assembly of the dystrophin glycoprotein complex - NatureA structural study of native dystrophin glycoprotein complex from mouse skeletal muscle reveals an extended tower-like architecture that provides multiple binding sites on both sides of the membrane for signalling and effector molecules, reshaping our understanding of how the complex is assembled.