#cryoem — Public Fediverse posts

Molecular & Structural Biology Scientist (Internship to Hire)
BalanX Bio

See the full job description on jobRxiv: https://jobrxiv.org/job/balanx-bio-27779-molecular-structural-biology-scientist/

#cryoEM #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/balanx-bio-27779-molecular-structural-biology-scientist/?fsp_sid=12507

New Title Alert: CryoBoltz- is a method for fitting atomic structures into cryo-EM density maps of dynamic proteins. It is built on top of Boltz-1, a state-of-the-art structure prediction model for biomolecular complexes.

Learn more here: https://cryoboltz.cs.princeton.edu/

#SBGrid #Software #CryoEM

RE: https://fediscience.org/@Guillawme/115798148618761432

This article on an ALC1-nucleosome complex with a new conformation was accepted at @ActaCrystD in April and went online today! Check it out!

https://doi.org/10.1107/S2059798326004158

#CryoEM #StructuralBiology #nucleosome #chromatin

Just found and #EMDB entry deposited in July 2020 without half-maps. 😮 I didn't know half-maps had been optional for so long...

#CryoEM

Just found and #EMDB entry deposited in July 2020 without half-maps. 😮 I didn't know half-maps had been optional for so long...

#CryoEM

Just found and #EMDB entry deposited in July 2020 without half-maps. 😮 I didn't know half-maps had been optional for so long...

#CryoEM

Just found and #EMDB entry deposited in July 2020 without half-maps. 😮 I didn't know half-maps had been optional for so long...

#CryoEM

Just found and #EMDB entry deposited in July 2020 without half-maps. 😮 I didn't know half-maps had been optional for so long...

#CryoEM

Postdoctoral Associate in Membrane Protein Structural Biology & Biophysics
Duke University School of Medicine

See the full job description on jobRxiv: https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/

#cellularbiophysics #cryoEM #ionchannels #membranep...
https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/?fsp_sid=12185

Postdoctoral Associate in Membrane Protein Structural Biology & Biophysics
Duke University School of Medicine

See the full job description on jobRxiv: https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/

#cellularbiophysics #cryoEM #ionchannels #membranep...
https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/?fsp_sid=12185

RE: https://biologists.social/@biorxiv_molbio/116541272170828580

Nice preprint! Two new things:

1. A user-friendly workflow for low-dose data collection setup in SerialEM. Very nice to have an "easy mode" for SerialEM. 🙏

2. An atomic resolution #cryoEM structure of apoferritin at ~1.1 Å, with a R&H B-factor *3-fold* improved compared to the atomic res ApoF structures from 2020. 🤯 🤩
EMD-57470 and EMPIAR-13508

I am really puzzled why the first result defined the paper, and not the second one, but it's impressive either way!

RE: https://biologists.social/@biorxiv_biochem/116556723014784898

Very interesting to see that it is the same "difficult" particles that trip up classification methods with completely different underlying formalism. Also great to now have a #cryoEM dataset with known ground truth assignments!

Oh I really didn't need a data storage crisis today... 🫠 🫠 🫠

#CryoEM

Some questions for people into #cryoEM and #biochemistry

All pKa values vary with temperature. This is especially apparent with Tris buffer: change of ~ +0.5 pH unit going from room temp to 4°C.

Proton transfers in acid/base equilibria are very fast. Are they faster than vitrification? In other words, does a change of pKa (due to a rapid drop in temperature) of the buffer compound have the time to change the pH of the solution before it is fully vitrified?

There are pH-sensitive fluorophores. Has anyone vitrified and imaged them in a cryo-confocal microscope to determine whether vitrification changed the pH?

Fisk University student Cariuna Ellison's highlight features an eLife publication from Jochen Zimmer's group at University of Virginia School of Medicine that describes the use of Cryo-EM to reveal how CvHAS utilizes a two-step mechanism to navigate the balance between substrate specificity and degeneracy.

Read more here: https://medium.com/sbgrid-community-news/molecular-proofreading-mechanisms-of-enzyme-binding-567ed3b5c4f2

#SBGrid #CryoEM #Binding

Fisk University student Cariuna Ellison's highlight features an eLife publication from Jochen Zimmer's group at University of Virginia School of Medicine that describes the use of Cryo-EM to reveal how CvHAS utilizes a two-step mechanism to navigate the balance between substrate specificity and degeneracy.

Read more here: https://medium.com/sbgrid-community-news/molecular-proofreading-mechanisms-of-enzyme-binding-567ed3b5c4f2

#SBGrid #CryoEM #Binding

Fisk University student Cariuna Ellison's highlight features an eLife publication from Jochen Zimmer's group at University of Virginia School of Medicine that describes the use of Cryo-EM to reveal how CvHAS utilizes a two-step mechanism to navigate the balance between substrate specificity and degeneracy.

Read more here: https://medium.com/sbgrid-community-news/molecular-proofreading-mechanisms-of-enzyme-binding-567ed3b5c4f2

#SBGrid #CryoEM #Binding

There’s a motor on this thing’s tail. 🦠⚙️
Scientists studied it for 50 years. Last month? They finally figured out how it spins.
The bacterial flagellar motor. 45 nanometers wide. 30 proteins, self-assembled. Runs on protons, not batteries. Reverses direction instantly.
After 50 years of work, one researcher said: "My lifelong pursuit is now realized."
Nature’s nano-engineering. Absolute perfection.

#BacterialMotor #MolecularBiology #CryoEM #NatureEngineering #ScienceBreakthrough #FlagellarMotor

There’s a motor on this thing’s tail. 🦠⚙️
Scientists studied it for 50 years. Last month? They finally figured out how it spins.
The bacterial flagellar motor. 45 nanometers wide. 30 proteins, self-assembled. Runs on protons, not batteries. Reverses direction instantly.
After 50 years of work, one researcher said: "My lifelong pursuit is now realized."
Nature’s nano-engineering. Absolute perfection.

#BacterialMotor #MolecularBiology #CryoEM #NatureEngineering #ScienceBreakthrough #FlagellarMotor

There’s a motor on this thing’s tail. 🦠⚙️
Scientists studied it for 50 years. Last month? They finally figured out how it spins.
The bacterial flagellar motor. 45 nanometers wide. 30 proteins, self-assembled. Runs on protons, not batteries. Reverses direction instantly.
After 50 years of work, one researcher said: "My lifelong pursuit is now realized."
Nature’s nano-engineering. Absolute perfection.

#BacterialMotor #MolecularBiology #CryoEM #NatureEngineering #ScienceBreakthrough #FlagellarMotor

There’s a motor on this thing’s tail. 🦠⚙️
Scientists studied it for 50 years. Last month? They finally figured out how it spins.
The bacterial flagellar motor. 45 nanometers wide. 30 proteins, self-assembled. Runs on protons, not batteries. Reverses direction instantly.
After 50 years of work, one researcher said: "My lifelong pursuit is now realized."
Nature’s nano-engineering. Absolute perfection.

#BacterialMotor #MolecularBiology #CryoEM #NatureEngineering #ScienceBreakthrough #FlagellarMotor

There’s a motor on this thing’s tail. 🦠⚙️
Scientists studied it for 50 years. Last month? They finally figured out how it spins.
The bacterial flagellar motor. 45 nanometers wide. 30 proteins, self-assembled. Runs on protons, not batteries. Reverses direction instantly.
After 50 years of work, one researcher said: "My lifelong pursuit is now realized."
Nature’s nano-engineering. Absolute perfection.

#BacterialMotor #MolecularBiology #CryoEM #NatureEngineering #ScienceBreakthrough #FlagellarMotor

The last couple of weeks, I was busy preparing for the #CCPEM Spring Symposium and then attending it and presenting at it. So I am only finding time now to share a new preprint that went online earlier this month: https://doi.org/10.64898/2026.04.02.716132

It is about the regulation of CsoSCA, the carbonic anhydrase (CA) found in alpha-carboxysomes. Through a combination of stopped-flow #kinetics, #bioinformatics and #cryoEM, we showed that this enzyme is sensitive to redox conditions. This likely keeps it inactive in the reducing cytosol, where CA activity would short-circuit the CO2 concentration mechanism by turning cytosolic bicarbonate into CO2, which can diffuse through membranes. This redox sensitivity also activates CsoSCA inside mature carboxysomes, because their interior becomes oxidizing as their shell excludes cytosolic reductants.
Overall, CsoSCA's redox sensitivity conditions its activation to its correct encapsulation in carboxysomes.

Turns out visualizing a regulatory disulfide by #cryoEM is difficult! In this case, the strongest evidence for it comes from activity measurements and site-directed mutagenesis. But the structures revealed a conformational equilibrium that we would not have suspected, had we not attempted to solve structures of the enzyme in the active and inactive conditions.

This was excellent team work with first author Nikole and all others, with a real cross-talk between the biochemistry and structures!

The last couple of weeks, I was busy preparing for the #CCPEM Spring Symposium and then attending it and presenting at it. So I am only finding time now to share a new preprint that went online earlier this month: https://doi.org/10.64898/2026.04.02.716132

It is about the regulation of CsoSCA, the carbonic anhydrase (CA) found in alpha-carboxysomes. Through a combination of stopped-flow #kinetics, #bioinformatics and #cryoEM, we showed that this enzyme is sensitive to redox conditions. This likely keeps it inactive in the reducing cytosol, where CA activity would short-circuit the CO2 concentration mechanism by turning cytosolic bicarbonate into CO2, which can diffuse through membranes. This redox sensitivity also activates CsoSCA inside mature carboxysomes, because their interior becomes oxidizing as their shell excludes cytosolic reductants.
Overall, CsoSCA's redox sensitivity conditions its activation to its correct encapsulation in carboxysomes.

Turns out visualizing a regulatory disulfide by #cryoEM is difficult! In this case, the strongest evidence for it comes from activity measurements and site-directed mutagenesis. But the structures revealed a conformational equilibrium that we would not have suspected, had we not attempted to solve structures of the enzyme in the active and inactive conditions.

This was excellent team work with first author Nikole and all others, with a real cross-talk between the biochemistry and structures!

The last couple of weeks, I was busy preparing for the #CCPEM Spring Symposium and then attending it and presenting at it. So I am only finding time now to share a new preprint that went online earlier this month: https://doi.org/10.64898/2026.04.02.716132

It is about the regulation of CsoSCA, the carbonic anhydrase (CA) found in alpha-carboxysomes. Through a combination of stopped-flow #kinetics, #bioinformatics and #cryoEM, we showed that this enzyme is sensitive to redox conditions. This likely keeps it inactive in the reducing cytosol, where CA activity would short-circuit the CO2 concentration mechanism by turning cytosolic bicarbonate into CO2, which can diffuse through membranes. This redox sensitivity also activates CsoSCA inside mature carboxysomes, because their interior becomes oxidizing as their shell excludes cytosolic reductants.
Overall, CsoSCA's redox sensitivity conditions its activation to its correct encapsulation in carboxysomes.

Turns out visualizing a regulatory disulfide by #cryoEM is difficult! In this case, the strongest evidence for it comes from activity measurements and site-directed mutagenesis. But the structures revealed a conformational equilibrium that we would not have suspected, had we not attempted to solve structures of the enzyme in the active and inactive conditions.

This was excellent team work with first author Nikole and all others, with a real cross-talk between the biochemistry and structures!

The last couple of weeks, I was busy preparing for the #CCPEM Spring Symposium and then attending it and presenting at it. So I am only finding time now to share a new preprint that went online earlier this month: https://doi.org/10.64898/2026.04.02.716132

It is about the regulation of CsoSCA, the carbonic anhydrase (CA) found in alpha-carboxysomes. Through a combination of stopped-flow #kinetics, #bioinformatics and #cryoEM, we showed that this enzyme is sensitive to redox conditions. This likely keeps it inactive in the reducing cytosol, where CA activity would short-circuit the CO2 concentration mechanism by turning cytosolic bicarbonate into CO2, which can diffuse through membranes. This redox sensitivity also activates CsoSCA inside mature carboxysomes, because their interior becomes oxidizing as their shell excludes cytosolic reductants.
Overall, CsoSCA's redox sensitivity conditions its activation to its correct encapsulation in carboxysomes.

Turns out visualizing a regulatory disulfide by #cryoEM is difficult! In this case, the strongest evidence for it comes from activity measurements and site-directed mutagenesis. But the structures revealed a conformational equilibrium that we would not have suspected, had we not attempted to solve structures of the enzyme in the active and inactive conditions.

This was excellent team work with first author Nikole and all others, with a real cross-talk between the biochemistry and structures!

The last couple of weeks, I was busy preparing for the #CCPEM Spring Symposium and then attending it and presenting at it. So I am only finding time now to share a new preprint that went online earlier this month: https://doi.org/10.64898/2026.04.02.716132

It is about the regulation of CsoSCA, the carbonic anhydrase (CA) found in alpha-carboxysomes. Through a combination of stopped-flow #kinetics, #bioinformatics and #cryoEM, we showed that this enzyme is sensitive to redox conditions. This likely keeps it inactive in the reducing cytosol, where CA activity would short-circuit the CO2 concentration mechanism by turning cytosolic bicarbonate into CO2, which can diffuse through membranes. This redox sensitivity also activates CsoSCA inside mature carboxysomes, because their interior becomes oxidizing as their shell excludes cytosolic reductants.
Overall, CsoSCA's redox sensitivity conditions its activation to its correct encapsulation in carboxysomes.

Turns out visualizing a regulatory disulfide by #cryoEM is difficult! In this case, the strongest evidence for it comes from activity measurements and site-directed mutagenesis. But the structures revealed a conformational equilibrium that we would not have suspected, had we not attempted to solve structures of the enzyme in the active and inactive conditions.

This was excellent team work with first author Nikole and all others, with a real cross-talk between the biochemistry and structures!

This year again I was lucky to be able to attend the #CCPEM Spring Symposium in person.

So much exciting science is going on in the #cryoEM and #cryoET #teamTomo fields!

I was especially impressed with the progress in time-resolved perturbation and vitrification for single-particle cryoEM.

Modifying the bacterial strain led to cleaner bacterial expression of a synthetic BRIL antibody that facilitates protein structure determination via both crystallography and cryo-EM #CryoEM #XRayCrystallography #BRIL https://doi.org/10.1107/S2053230X26001548

P2X receptors are ATP-gated #IonChannels that are targets for treating #ChronicPain & #cough. The #cryoEM structure of the human #P2X3 receptor in complex with the negative allosteric modulator sivopixant reveals how it stabilizes inhibitory conformations of P2X3 @PLOSBiology https://plos.io/4vMWCvy

P2X receptors are ATP-gated #IonChannels that are targets for treating #ChronicPain & #cough. The #cryoEM structure of the human #P2X3 receptor in complex with the negative allosteric modulator sivopixant reveals how it stabilizes inhibitory conformations of P2X3 @PLOSBiology https://plos.io/4vMWCvy

P2X receptors are ATP-gated #IonChannels that are targets for treating #ChronicPain & #cough. The #cryoEM structure of the human #P2X3 receptor in complex with the negative allosteric modulator sivopixant reveals how it stabilizes inhibitory conformations of P2X3 @PLOSBiology https://plos.io/4vMWCvy

P2X receptors are ATP-gated #IonChannels that are targets for treating #ChronicPain & #cough. The #cryoEM structure of the human #P2X3 receptor in complex with the negative allosteric modulator sivopixant reveals how it stabilizes inhibitory conformations of P2X3 @PLOSBiology https://plos.io/4vMWCvy

P2X receptors are ATP-gated #IonChannels that are targets for treating #ChronicPain & #cough. The #cryoEM structure of the human #P2X3 receptor in complex with the negative allosteric modulator sivopixant reveals how it stabilizes inhibitory conformations of P2X3 @PLOSBiology https://plos.io/4vMWCvy

Postdoc Positions - Structural Biology, Biochemistry, Cell Biology
University of Cincinnati

See the full job description on jobRxiv: https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/

#biochemistry #cellbiology #cryoEM #proteinbiochemistry #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/?fsp_sid=11241

Postdoc Positions - Structural Biology, Biochemistry, Cell Biology
University of Cincinnati

See the full job description on jobRxiv: https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/

#biochemistry #cellbiology #cryoEM #proteinbiochemistry #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/?fsp_sid=11241

Postdoc Positions - Structural Biology, Biochemistry, Cell Biology
University of Cincinnati

See the full job description on jobRxiv: https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/

#biochemistry #cellbiology #cryoEM #proteinbiochemistry #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/?fsp_sid=11241

Postdoc Positions - Structural Biology, Biochemistry, Cell Biology
University of Cincinnati

See the full job description on jobRxiv: https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/

#biochemistry #cellbiology #cryoEM #proteinbiochemistry #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/?fsp_sid=11241

Postdoc Positions - Structural Biology, Biochemistry, Cell Biology
University of Cincinnati

See the full job description on jobRxiv: https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/

#biochemistry #cellbiology #cryoEM #proteinbiochemistry #structuralbiology #ScienceJobs #hiring #research
https://jobrxiv.org/job/university-of-cincinnati-27778-postdoc-positions-structural-biology-biochemistry-cell-biology/?fsp_sid=11241

#Sphingosine -1-phosphate receptors #S1PRs play complex roles in several pathological processes. #CryoEM structures of four agonist-bound S1PR1-Gi1 complexes reveal the structural determinants underlying agonist selectivity among different subtypes @PLOSBiology https://plos.io/4co0A4W

The human G6P transporter (G6PT) translocates G6P into the #ER. This study solves hi-res #cryoEM structures of #G6PT in both outward-open & dimeric states, providing insights into the mechanistic basis for G6P substrate recognition & transport cycle @PLOSBiology https://plos.io/4m15UQ5

He also hinted at a new class of synthetic antibiotics that is in current development at Roche. Hopefully there are many more new antibiotics in the future. (7/7)

#Antibiotics #DrugDiscovery #DrugDevelopment #ChemBio #Chemistry #cryoEM #AMR #Resistance #Bacteria #SAR #Synthesis #Zosurabalpin

Here is a strong candidate for the coolest-looking #cryoEM structure of 2026! 🤩

Structural basis of supercoiling-induced CRISPR–Cas9 off-target activity

https://doi.org/10.1038/s41586-026-10255-7

#StructuralBiology

Postdoctoral Associate in Membrane Protein Structural Biology & Biophysics
Duke University School of Medicine

See the full job description on jobRxiv: https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/

#cellularbiophysics #cryoEM #ionchannels #membranep...
https://jobrxiv.org/job/duke-university-school-of-medicine-27778-postdoctoral-associate-in-membrane-protein-structural-biology-biophysics/?fsp_sid=10553

How do our muscles work on a molecular scale?

Stefan Raunser gave an inspiring lecture on his group's work at the Max Planck Institute of Molecular Physiology, in which they elucidate this question with a great combination of biochemistry and structural biology.

https://www.annualreviews.org/content/journals/10.1146/annurev-biochem-052521-042909
#Biochemistry #Structure #cryoEM #Chemistry #ChemBio
CC: @gdch, @GDCh_BioChem

How are the receptors in the synapse organized?

Diego Ortiz-López from the Hermann Schindelin group discussed his research at #Biochemistry2026. He talked about the organization of receptors in the inhibitory postsynapse by organization of gephyrin oligomers.

https://www.biorxiv.org/content/10.1101/2025.09.01.673457v1
#Biochemistry #cryoEM #Structure #Synapse #Chemistry #ChemBio
CC: @gdch, @GDCh_BioChem

Installation of tRNA modifications is key to protein synthesis.

In her presentation at #Biochemistry2026, Carine Tisné presented her group's in depth work on structural and functional studies to understand the underlying processes on the example of m1A.

https://pubs.acs.org/doi/10.1021/acs.accounts.3c00568
#Biochemistry #RNA #tRNA #Modification #ProteinSynthesis #Chemistry #ChemBio #cryoEM #Crystallography
CC: @gdch

Installation of tRNA modifications is key to protein synthesis.

In her presentation at #Biochemistry2026, Carine Tisné presented her group's in depth work on structural and functional studies to understand the underlying processes on the example of m1A.

https://pubs.acs.org/doi/10.1021/acs.accounts.3c00568
#Biochemistry #RNA #tRNA #Modification #ProteinSynthesis #Chemistry #ChemBio #cryoEM #Crystallography
CC: @gdch

Installation of tRNA modifications is key to protein synthesis.

In her presentation at #Biochemistry2026, Carine Tisné presented her group's in depth work on structural and functional studies to understand the underlying processes on the example of m1A.

https://pubs.acs.org/doi/10.1021/acs.accounts.3c00568
#Biochemistry #RNA #tRNA #Modification #ProteinSynthesis #Chemistry #ChemBio #cryoEM #Crystallography
CC: @gdch

Installation of tRNA modifications is key to protein synthesis.

In her presentation at #Biochemistry2026, Carine Tisné presented her group's in depth work on structural and functional studies to understand the underlying processes on the example of m1A.

https://pubs.acs.org/doi/10.1021/acs.accounts.3c00568
#Biochemistry #RNA #tRNA #Modification #ProteinSynthesis #Chemistry #ChemBio #cryoEM #Crystallography
CC: @gdch