ArticleChemMedChem2025
Ligand Screening and Discovery Using Cocktail Soaking and Automated Microcrystal Electron Diffraction.
Article in ChemMedChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026Review
- Combining MicroED and native mass spectrometry for structural discovery of enzyme-small molecule complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
- Update of
Authors and funding
4 authors.
Funding
Abstract
Cocktail soaking using single-crystal X-ray diffraction previously allowed high-throughput crystallographic screening of ligands against protein targets. However, protein microcrystals are not amenable to this approach if they are too small to yield strong diffraction patterns. Herein, a workflow integrating cocktail soaking with automated microcrystal electron diffraction to allow rapid ligand screening, structure determination, and binding analysis directly from microcrystals is developed. This can improve the successful hit rate, because binding is often more efficient when smaller crystals are soaked in the ligand. The approach is validated with known ligands of thermolysin and identified novel binding interactions for ligands of proteinase K. The structures of multiple protein-ligand complexes, including ligands with weak binding affinities, can be solved rapidly. Their estimated relative binding affinities are in good agreement with previous work and independent microscale thermophoresis measurements.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.