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| Network | Status | Live ads | Nov 2025LinkedIn activity · 52 weeksOct 2026 | Checked | Next step |
|---|---|---|---|---|---|
| Running | 10 | Checked 30 Oct 2026 | See all 27 ads → | ||
| Meta | None recorded | 0 | No active ads recorded on the Meta Ad Library | Checked 19 Oct 2026 | Collect them with the API → |
| Running | 34 | Ads on the Google Ads Transparency Center | Checked 27 Oct 2026 | Collect them with the API → |
Direct Electron has 10 live LinkedIn ads. Its Facebook page had no active ads on 19 Oct 2026, and we recorded 34 Google ads on 27 Oct 2026.
Latest ads
- LINKEDIN · IMAGESince 28 Sept 2026
What does the highest-resolution biological structure ever solved look like — and what did it take to get there? We've put together a rundown of the top 5 biological molecular structures ever solved. Two of them were achieved by Micro-ED on a conventional TEM. No synchrotron required. The resolution numbers will surprise you. See the full list 👇 #StructuralBiology #DrugDiscovery #MicroED #CryoEM #Pharma #ProteinCrystallography
- LINKEDIN · IMAGESince 28 Sept 2026
The secret to higher resolution Cryo-EM structures might be in your beam settings! 🔑 Every day, countless hours are spent imaging proteins, but are you maximizing your data quality? The choice of dose rate—whether to use high beam intensity or longer time—has huge implications for the final resolution of your atomic models. Thankfully, FSU researchers have done the crucial work, providing a clear comparison of different dose rates to guide your experiments. See their findings and upgrade your Cryo-EM workflow today! 👇 #StructuralBiology #ProteinStructure #Microscopy #DataAcquisition #BestPractice
- LINKEDIN · IMAGESince 15 Jun 2026
What if the crystal structure you solved wasn't the structure your drug actually adopts in the body? 🔬 Conventional sample prep dries out hydrates, collapses solvated polymorphs, and hands you an artefact — not a structure. For pharmaceutical scientists, that's not an academic problem. It's a formulation risk. A new methodology changes that. Room-temperature liquid cell Micro-ED now allows atomic-resolution structure determination from microcrystals maintained in their native, hydrated state — no synchrotron access, no single-crystal growth, no months-long beamtime applications. Just a microcrystal slurry, standard TEM grids, and results in a day. If your work touches solid-state characterization, lead optimization, or structural analysis of pharmaceutical materials — this is worth 5 minutes of your time. 👇 #DrugDiscovery #PharmaceuticalScience #StructuralBiology #MicroED #SolidState #Crystallography #ElectronDiffraction #Formulation
- LINKEDIN · IMAGESince 13 Jun 2026
If you work on GPCRs, you already know the crystallization problem. Getting crystals large enough for synchrotron X-ray data is one of the most punishing bottlenecks in GPCR structural biology — and it doesn't have to be. Micro-ED only needs a single microcrystal of ~300nm or larger. That's a fundamentally different crystallization target — one that's actually achievable for GPCRs in lipid cubic phase. We asked experts in protein crystallography and drug discovery how they make it work. The result is a practical 5-tip guide for anyone trying to solve GPCR structures in-house. 👇 Check it out below. #StructuralBiology #GPCR #DrugDiscovery #MicroED #StructureBasedDrugDesign #Pharma
- LINKEDIN · IMAGESince 12 Jun 2026
What if your TEM could identify the best crystals, collect diffraction data, and solve a structure — without anyone at the controls? REyes, developed at Caltech, does exactly that. And for pharma structural biology groups running micro-ED, the throughput and resolution implications are significant. Micro-ED has always promised more than it delivered at scale. REyes removes the bottleneck that's held it back. Find out how 👇 #StructuralBiology #DrugDiscovery #MicroED #CryoEM #Pharma #Structure #ProteinCrystallography
- LINKEDIN · IMAGESince 8 Jun 2026
Research paper from Florida State University finds large differences in resolution for different dose rates.
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