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Hannah R Bridges

@hrbridges

Biochemist and Structural Biologistβ„οΈπŸ”¬, occasional artist, keeper of orchids, converted cat person 🐾| all views my own

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08.01.2024
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Latest posts by Hannah R Bridges @hrbridges

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πŸš€ CryoSPARC v5.0 BETA is here!

We’re excited to deploy another major #CryoSPARC release to help enable and accelerate #cryoEM data analysis. v5 has a redesigned underlying software system and many new features - highlights in thread!

Full changelog: cryosparc.com/updates/v5.0.0

27.01.2026 20:36 πŸ‘ 67 πŸ” 34 πŸ’¬ 1 πŸ“Œ 1
Original post on fediscience.org

RE: https://fediscience.org/@Guillawme/111534984107819771

Something really cool happened to me this year!

@HRBridges re-processed a #cryoEM dataset from some previous work of mine and colleagues (publicly available as EMPIAR-10739; see quoted post below for a summary of this work). She […]

28.12.2025 16:32 πŸ‘ 13 πŸ” 8 πŸ’¬ 3 πŸ“Œ 0
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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 πŸ‘ 9 πŸ” 14 πŸ’¬ 0 πŸ“Œ 0

ALC1 Finds a New Foothold on the Nucleosome's Super-Groove https://www.biorxiv.org/content/10.1101/2025.11.10.687450v1

11.11.2025 02:48 πŸ‘ 3 πŸ” 3 πŸ’¬ 0 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 πŸ‘ 32 πŸ” 11 πŸ’¬ 0 πŸ“Œ 1
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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 πŸ‘ 65 πŸ” 21 πŸ’¬ 1 πŸ“Œ 3
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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 πŸ‘ 16 πŸ” 5 πŸ’¬ 0 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 πŸ‘ 25 πŸ” 5 πŸ’¬ 0 πŸ“Œ 0
Characterised members of the human SLC25 mitochondrial family. Members of the mitochondrial carriers are shown in rainbow (blue to red) cartoon and surface representations with their primary substrates shown in sphere representations to scale. Only one paralogue is shown.

Characterised members of the human SLC25 mitochondrial family. Members of the mitochondrial carriers are shown in rainbow (blue to red) cartoon and surface representations with their primary substrates shown in sphere representations to scale. Only one paralogue is shown.

Our review on the peculiar properties of mitochondrial carriers of the SLC25 family out: portlandpress.com/biochemj/art...

25.07.2025 11:29 πŸ‘ 32 πŸ” 9 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 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 πŸ‘ 34 πŸ” 11 πŸ’¬ 0 πŸ“Œ 0

A really insightful piece, Christian :) I used to think on this topic often. It will be interesting to see how things change for individuals and for the system, as more people realise the toll that such professional and personal dissonance can have.

10.05.2025 12:40 πŸ‘ 3 πŸ” 0 πŸ’¬ 0 πŸ“Œ 0
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The Professional Self: The Enemy Inside

I'd like to share this short piece on a topic I hope you will find useful. It is the result of a personl journey and many discussions with friends and peers. Let me know your thoughts.

network.febs.org/posts/the-pr...

09.05.2025 18:05 πŸ‘ 44 πŸ” 15 πŸ’¬ 8 πŸ“Œ 8
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Well, somebody had to do it @nucleosomepolice.bsky.social 😬

Did you know that the nucleosome inspires the Millennium Falcon design? #Maythe4thBeWithYou #MayThe4th #MayTheFourthBeWithYou

04.05.2025 06:30 πŸ‘ 104 πŸ” 22 πŸ’¬ 3 πŸ“Œ 3
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Grappling with poorly-resolved ligand binding sites in #cryoEM maps?
Check out our new case study on a peptide ligand-bound GPCR showing how practical tips and features in #CryoSPARC v4.7 improve locally refined map quality and reveal clearer ligand density!
guide.cryosparc.com/processing-d...

29.04.2025 15:22 πŸ‘ 32 πŸ” 7 πŸ’¬ 0 πŸ“Œ 0
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Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier The mitochondrial pyruvate carrier transport mechanism is Ξ”pH driven and is inhibited competitively by distinct compound classes.

Our paper is finally out: Molecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier | Science Advances www.science.org/doi/10.1126/...
#mitochondria #cryo-EM

18.04.2025 18:16 πŸ‘ 43 πŸ” 13 πŸ’¬ 2 πŸ“Œ 0
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#CryoSPARC v4.7 is out! πŸš€Β 
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

09.04.2025 14:14 πŸ‘ 52 πŸ” 19 πŸ’¬ 1 πŸ“Œ 2

Check out our recent preprint πŸ‘‡on counting particles to estimate populations in #cryoem: noise can bias the estimates; with Luke Evans & a great team.

30.03.2025 13:29 πŸ‘ 29 πŸ” 13 πŸ’¬ 0 πŸ“Œ 1
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Structure of Mycobacterial NDH-2 Bound to a 2-Mercapto-Quinazolinone Inhibitor Mycobacterial type II NADH dehydrogenase (NDH-2) is a promising drug target because of its central role in energy metabolism in Mycobacterium tuberculosis and other pathogens, and because it lacks a k...

Now published J. Med. Chem! @zestytoast.bsky.social's structure of type II NADH dehydrogenase from mycobacteria. A promising drug target for TB & other mycobacterial infections, Yingke demonstrates how an inhibitor can block transfer of electrons from NADH to the ETC.
pubs.acs.org/doi/full/10....

21.03.2025 16:55 πŸ‘ 24 πŸ” 10 πŸ’¬ 2 πŸ“Œ 0
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In a new Science study, cryo–electron tomography captures the in-cell architecture of the mitochondrial respiratory chain, illuminating how the coordinated action of molecular machines drives life’s fundamental energy conversion.

Learn more in this week's issue: scim.ag/3FA3Ygq

20.03.2025 18:05 πŸ‘ 463 πŸ” 144 πŸ’¬ 15 πŸ“Œ 35

Awesome and exciting times @macleanlab.bsky.social !

27.02.2025 18:39 πŸ‘ 4 πŸ” 0 πŸ’¬ 1 πŸ“Œ 0
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We are hosting a cryo-EM grid nanofabrication workshop on 28 April 2025, as part of the Canadian Cryo-EM Nexus (ccemn.ca).
Learn how to make holey gold or holey carbon grids in your own laboratory!
Space is limited, so please apply at web.cvent.com/event/ee88ac...

06.01.2025 19:28 πŸ‘ 46 πŸ” 31 πŸ’¬ 3 πŸ“Œ 1

Finally out! Working with this team was a fantastic learning experience. Also I was excited to determine the in situ clathrin structure for this project! That’s my first EM-structure upload to EMDB. Can I tell my mom I am a structural biologist now? 😁 #cryoET

06.01.2025 18:00 πŸ‘ 38 πŸ” 4 πŸ’¬ 1 πŸ“Œ 1
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Distinct roles for the domains of the mitochondrial aspartate/glutamate carrier citrin in organellar localization and substrate transport Citrin, the mitochondrial aspartate/glutamate carrier isoform 2 (AGC2), is structurally and mechanistically the most complex SLC25 family member, beca…

Using 33 pathogenic variants of citrin we identify crucial elements of the carrier domain required for transport and show that the N-terminal domain is not involved in calcium regulation of transport, but causes a mitochondrial import defect, when mutated.
www.sciencedirect.com/science/arti...

01.12.2024 12:47 πŸ‘ 6 πŸ” 2 πŸ’¬ 0 πŸ“Œ 0
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2024 S2C2 Single-Particle Cryo-EM Image Processing Workshop - YouTube This playlist contains six recordings covering single particle cryo-EM data processing in CryoSPARC from the 2024 Single-Particle Cryo-EM Image Processing Wo...

1/ A new series of #CryoSPARC tutorial videos from this year’s S2C2 #cryoEM image processing workshop are now online! These videos will be interesting to all users and especially those newer to #cryoEM.

www.youtube.com/playlist?lis...

13.12.2024 18:56 πŸ‘ 63 πŸ” 30 πŸ’¬ 3 πŸ“Œ 2
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Looking for a primer on why the contrast transfer function matters in #cryoEM?

Have a look at our updated #CryoSPARC Guide pages on CTF estimation! We cover intuition, theory, job types and practical considerations: guide.cryosparc.com/processing-d...

09.12.2024 21:24 πŸ‘ 34 πŸ” 17 πŸ’¬ 0 πŸ“Œ 0
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Just for fun, reprocessed a subset (1200 mics) of EMPIAR-11918 (beautiful 40kDa RNA-protein complex) with cryoSPARC to compare with BLUSH/RELION workflow - 3Γ… NU-refine from 60k blob-picked particles after quick classification without alignments

06.12.2024 03:25 πŸ‘ 47 πŸ” 9 πŸ’¬ 2 πŸ“Œ 0
bioRxiv Manuscript Processing System Manuscript Processing System for bioRxiv.

Finally we are able to share our story on the molecular mechanism of the transformative anti-tuberculosis drug bedaquiline within living cells

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

A (hopefully) broadly-accessible tutorial below ⬇️ (it ended up being really long!)

05.12.2024 22:16 πŸ‘ 46 πŸ” 16 πŸ’¬ 3 πŸ“Œ 4
Cryo-EM map and atomic model of the RAVE complex (regulator of ATPases of endosomes and vacuoles) bound to a partial V1-ATPase complex

Cryo-EM map and atomic model of the RAVE complex (regulator of ATPases of endosomes and vacuoles) bound to a partial V1-ATPase complex

Atomic model showing that the RAVE complex binds to a region of the V1 complex subunit A not found in the homologous ATP synthase subunit beta.

Atomic model showing that the RAVE complex binds to a region of the V1 complex subunit A not found in the homologous ATP synthase subunit beta.

Most protein complexes are born only once. V-ATPase assembles over and over as part of its regulatory mechanism, enabled by RAVE (regulator of ATPase of vacuoles and endosomes)
@hanlinw222.bsky.social's 1st struct of RAVE bound to a partial V1 complex now out in PNAS.
www.pnas.org/doi/10.1073/...

03.12.2024 19:34 πŸ‘ 62 πŸ” 14 πŸ’¬ 1 πŸ“Œ 0

Scientists, academics, researchers: We’re excited to share that @altmetric.com is now tracking mentions of your research on Bluesky! πŸ§ͺ

03.12.2024 14:10 πŸ‘ 29668 πŸ” 5025 πŸ’¬ 458 πŸ“Œ 280