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Structura Biotechnology

@structurabio.bsky.social

Algorithms, Software and Systems for Cryo-EM. Makers of CryoSPARC.

1,112 Followers  |  816 Following  |  29 Posts  |  Joined: 13.11.2024  |  2.0196

Latest posts by structurabio.bsky.social on Bluesky

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Structura Bio | Structura Bio

πŸš€ Hiring: Cryo-EM Application Scientist, Marketing!

Develop and deliver high-impact scientific marketing content, illustrate the value of new #CryoSPARC features and #cryoEM advances, and help scientists understand how our tools can help solve their problems.

structura.bio/careers/appl...

20.11.2025 21:00 β€” πŸ‘ 9    πŸ” 14    πŸ’¬ 0    πŸ“Œ 0
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CAHRA 2025: Community-Wide Assessment of Cryo-EM Heterogeneous Reconstruction Algorithms A community-wide data processing challenge for cryo-electron microscopy.

Announcing cryo-EM heterogeneity challenge #2, now dubbed the 2025 Community-Wide Assessment of Cryo-EM Heterogeneous Reconstruction Algorithms (CAHRA)! Join us for a webinar next Friday (Nov 14th) to learn more. Datasets already posted here: heterogeneity.notion.site/challenge #cryoem

07.11.2025 22:45 β€” πŸ‘ 8    πŸ” 11    πŸ’¬ 0    πŸ“Œ 0
Cryo-EM maps and atomic models of the biotin-containing 3-methylcrotonyl-CoA carboxylase (MCC) complex and long-chain acyl-CoA carboxylase (LCC) complex

Cryo-EM maps and atomic models of the biotin-containing 3-methylcrotonyl-CoA carboxylase (MCC) complex and long-chain acyl-CoA carboxylase (LCC) complex

New lab preprint!
@zestytoast.bsky.social tagged a scarce mycobacterial protein in M. smegmatis with TwinStep but got… something? @kjamali.bsky.social's ModelAngelo built models & @martinsteinegger.bsky.social's FoldSeek IDed them as the biotin-containing MCC & LCC complexes
🧡
tinyurl.com/ukny4ptz

30.10.2025 03:21 β€” πŸ‘ 82    πŸ” 29    πŸ’¬ 3    πŸ“Œ 1
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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...

30.10.2025 13:33 β€” πŸ‘ 32    πŸ” 11    πŸ’¬ 0    πŸ“Œ 1
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CryoSPARC | Automated Repeat‑Target Structure Determination An end‑to‑end, automated workflow for single‑particle cryo‑EM that achieves state‑of‑the‑art consensus maps suitable for model buildingβ€”demonstrated across 21 GPCR datasets, meeting or exceeding publi...

At cryosparc.com/automated-workflows we provide instructions and CryoSPARC Workflow JSON files so that users can get started with automation easily.
Reach out at discuss.cryosparc.com/c/automated-workflows.
Happy processing!

20.10.2025 14:32 β€” πŸ‘ 5    πŸ” 0    πŸ’¬ 0    πŸ“Œ 0

Automated processing unlocks several benefits. Time-to-structure can be greatly reduced and throughput can be easily scaled for repeat-target use cases. Solving multiple structures per day can now become a reality. πŸš€

20.10.2025 14:32 β€” πŸ‘ 4    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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The workflow is powered by new methods, including micrograph junk detection, denoising, and reference based auto selection of 2D classes and 3D volumes. Read the preprint for more insights and details.

20.10.2025 14:32 β€” πŸ‘ 2    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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The automated workflow generalizes easily to new target classes.
We provide downloadable #CryoSPARC Workflow JSON files so that users can replicate, adapt and extend it for their own targets. All required jobs and tools are already available in v4.7.1+.

20.10.2025 14:32 β€” πŸ‘ 2    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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In 10 of 21 cases, the automated results enable improved model building of the ligand, binding pocket, side chain positioning and/or extracellular loops. Three striking examples are shown here and in the first video.

20.10.2025 14:32 β€” πŸ‘ 2    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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We test across 21 challenging active and inactive GPCR datasets.
Despite small particle size and the presence of contaminants, empty micelles, broken, denatured and aggregated particles, our automated workflow yields equal or better resolution and map quality in 17 of 21 cases.

20.10.2025 14:32 β€” πŸ‘ 1    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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The automation strategy we have developed can be set up once for any specific target class (e.g. active state GPCRs with Nb35) and reused to process multiple datasets fully hands-off. It makes use of minimal prior knowledge through a low-res (15Γ…) 3D reference map.

20.10.2025 14:32 β€” πŸ‘ 2    πŸ” 0    πŸ’¬ 1    πŸ“Œ 0
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πŸš€ Introducing fully automated data processing for repeat-target #cryoEM.

Using new tools in #CryoSPARC, it is now possible to obtain resolutions & map quality equal to or better than manual processing, with zero user intervention.

Preprint: www.biorxiv.org/content/10.1...

20.10.2025 14:32 β€” πŸ‘ 65    πŸ” 21    πŸ’¬ 1    πŸ“Œ 3

End-to-end automation of repeat-target cryo-EM structure determination in CryoSPARC https://www.biorxiv.org/content/10.1101/2025.10.17.682689v1

20.10.2025 13:47 β€” πŸ‘ 10    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
Amyloid reconstructions from cryoSPARC

Amyloid reconstructions from cryoSPARC

Helical Reconstruction of Amyloids in cryoSPARC?
We present guidelines, limitations & future perspectives for processing amyloids in cryoSPARC @structurabio.bsky.social.
Great collaboration of the Kelly Lab and @landerlab.bsky.social #cryoEM #amyloid www.biorxiv.org/content/10.1...

05.10.2025 04:16 β€” πŸ‘ 44    πŸ” 14    πŸ’¬ 3    πŸ“Œ 0
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Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters - Nature Structural & Molecular Biology Reddy et al. used ancestral protein reconstruction, cryo-electron microscopy and functional assays to elucidate how a secondary active transporter evolved to harness the energy of sodium gradients to ...

1/14
Happy (but mostly relieved) to share my dream project with @boudkerlab.bsky.social, now published in @natsmb.nature.com! We used evolution, protein engineering & cryoEM to uncover how ion coupling in glutamate transporters works, and how it evolved.🧡
Free article: go.nature.com/4oRUC1q

12.09.2025 00:07 β€” πŸ‘ 22    πŸ” 8    πŸ’¬ 1    πŸ“Œ 2

This one is a bit of a departure from the usual and definitely a work in progress!

We found that by using ab initio reconstruction at very high res, in very small steps, we could crack some small structures that had eluded us - e.g. 39kDa iPKAc (EMPIAR-10252), below.

Read on for details... 1/x

13.09.2025 00:04 β€” πŸ‘ 265    πŸ” 82    πŸ’¬ 19    πŸ“Œ 14
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Advanced #cryoEM workflows are easy in #CryoSPARC: use the Low-Level Results Interface to combine upstream extracted particles with downstream pose and CTF information, use a volume result from an intermediate iteration of a refinement to create a mask, and more! guide.cryosparc.com/application-...

10.09.2025 15:46 β€” πŸ‘ 16    πŸ” 5    πŸ’¬ 0    πŸ“Œ 1
Upper - cryo-EM reconstruction of stomatin AQP1 complex. Lower - reconstruction of stomatin-UT-B complex.

Upper - cryo-EM reconstruction of stomatin AQP1 complex. Lower - reconstruction of stomatin-UT-B complex.

Happy to share a new preprint from the Clarke & Vallese (@fravallese.bsky.social) labs reporting #cryoem structures of two RBC stomatin complexes – with AQP1 & UT-B - continuing the SPFH theme from our recent vault preprint! This was a fun one and has been cooking for a while - read on for more! ⬇️

30.08.2025 14:10 β€” πŸ‘ 119    πŸ” 30    πŸ’¬ 8    πŸ“Œ 7
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Welcome! You are invited to join a webinar: Soluble Proteins in Focus: Preparing for Cryo-EM Success. After registering, you will receive a confirmation email about joining the webinar. Are you using cryo-EM to look at small soluble proteins? Join Dr. Claudio Catalano, a Senior Scientist at NanoImaging Services, to get expert advice on how to set your project up for success. He wil...

πŸ§ͺ Skip the trial and error for structure determination of soluble proteins. Join the #webinar 10/8 for a gene-to-structure case study of CYP3A4, a 57 kDa cytochrome P450 monooxygenase, solved to 3.1 Γ… by #cryoEM.

nimgs.zoom.us/webinar/regi...

27.08.2025 18:12 β€” πŸ‘ 5    πŸ” 4    πŸ’¬ 0    πŸ“Œ 0
Quote from Dr. Mingda Ye, University of Oxford, highlighting the collaborative breakthrough in cryo-EM imaging of small proteins: β€œThis idea was initiated when solving sub-50kDa protein structures by cryo-EM was almost impossible. To break this barrier, many world-class scientists in different fields have combined forces and it is a great honour to work with them to bring this game-changing tool into reality!” The background diagram outlines the scientific workflow used in the study.

Quote from Dr. Mingda Ye, University of Oxford, highlighting the collaborative breakthrough in cryo-EM imaging of small proteins: β€œThis idea was initiated when solving sub-50kDa protein structures by cryo-EM was almost impossible. To break this barrier, many world-class scientists in different fields have combined forces and it is a great honour to work with them to bring this game-changing tool into reality!” The background diagram outlines the scientific workflow used in the study.

Exciting work from the Franklin, @ox.ac.uk, and @diamondlightsource.bsky.social has led to a new method for imaging small proteins (<50 kDa) using cryoEM. By using bifunctional, bispecific nanobody scaffolds, the team have successfully solved the smallest protein structure to date (14 kDa).

18.08.2025 15:27 β€” πŸ‘ 13    πŸ” 8    πŸ’¬ 1    πŸ“Œ 0
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Covalently constrained β€˜Di-Gembodies’ enable parallel structure solutions by cryo-EM - Nature Chemical Biology Disulfide-based dimerization of modified identical and heterologous nanobody scaffolds enables higher-order assembly for high-resolution cryo-electron microscopy structure determination that is widely...

Di-Gembodies (dimerized nanobodies) for improved and duplexed CryoEM of small and challenging targets!

A collaboration of @cmd.ox.ac.uk, STRUBI, @diamondlightsource.bsky.social, @rosfrankinst.bsky.social

Out now in Nature Chemical Biology @natchembio.nature.com

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

15.08.2025 10:00 β€” πŸ‘ 36    πŸ” 22    πŸ’¬ 0    πŸ“Œ 1
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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...

15.08.2025 21:26 β€” πŸ‘ 60    πŸ” 19    πŸ’¬ 1    πŸ“Œ 1
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Flexibility can be frustrating when processing a #cryoEM dataset. If your target has a wobbly domain, check out our new case study on FaNaC1 for continuous heterogeneity tips in #CryoSPARC!

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

05.08.2025 13:46 β€” πŸ‘ 25    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
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Cryo electron microscopy and 3D image processing (CEM3DIP) This EMBO Practical Course is for participants who are interested in analysis of macromolecular structures in vitro and in situ using cryo-electron microscopy single particle reconstruction and t…

Get hands-on training on #cryofreezing, #DataAcquisition and more at EMBO Practical Course "Cryo electron microscopy and 3D image processing" in New Delhi, IN, 21 Feb–3 Mar 2026

Registration by 15 Sep
Abstract submission by 30 Sep

meetings.embo.org/event/26-cem...
#cryoEM #EMBOCryo3D #EMBOevents πŸ§ͺ

29.07.2025 09:50 β€” πŸ‘ 7    πŸ” 4    πŸ’¬ 0    πŸ“Œ 0

That's a wrap! The results of the first #cryoEM heterogeneity challenge are up on biorxiv!
biorxiv.org/content/10.110

23.07.2025 21:43 β€” πŸ‘ 45    πŸ” 22    πŸ’¬ 3    πŸ“Œ 4
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When particles have orientation bias, the resulting maps are often streaked along the missing directions. In this case study, we cover why orientation bias produces anisotropic #cryoEM maps and how you may be able to recover from it!

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

23.07.2025 12:29 β€” πŸ‘ 34    πŸ” 11    πŸ’¬ 0    πŸ“Œ 0
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Case Study: Pseudosymmetry in TRPV5 and Calmodulin (EMPIAR-10256) | CryoSPARC Guide Processing EMPIAR-10256 with a focus on handling pseudosymmetry and 3D Classification parameter choices.

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

14.07.2025 17:43 β€” πŸ‘ 1    πŸ” 0    πŸ’¬ 0    πŸ“Œ 0

Link here! guide.cryosparc.com/processing-d...

14.07.2025 17:43 β€” πŸ‘ 12    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0
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Working with symmetric or pseudosymmetric particles in #cryoEM?

This TRPV5 and CaM case study includes practical considerations for using symmetry relaxation and 3D classification when analyzing a pseudosymmetric particle in #CryoSPARC!

14.07.2025 12:48 β€” πŸ‘ 20    πŸ” 6    πŸ’¬ 2    πŸ“Œ 2

When I arrived to NYC as a postdoc, NYSBDG was my first local meeting, and I was blown way by the world-class quality of the science.

It's a great opportunity to meet the local #structbio & #cryoem community, and it's coming up in two weeks, so register now at the eventbrite link below!

07.07.2025 14:13 β€” πŸ‘ 7    πŸ” 5    πŸ’¬ 0    πŸ“Œ 0

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