ArticleActa crystallographica. Section D, Structural biology2020
FragMAX: the fragment-screening platform at the MAX IV Laboratory.
Article in Acta crystallographica. Section D, Structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Article
- Developments and challenges in hit progression within fragment-based drug discovery.Nature communications · 2026Review
- Crystallographic fragment screening supports tool compound discovery and reveals conformational flexibility in human deoxyhypusine synthase.Communications chemistry · 2026Article
- Deep learning for robust orbit control of Elettra 2.0 storage ring.Scientific reports · 2025Article
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Project automation in CCP4 Cloud: Enabling customization and high-throughput efficiency.Protein science : a publication of the Protein Society · 2025Article
- Where and how to house big data on small fragments.Nature communications · 2025Review
- Status and perspective of protein crystallography at the first multi-bend achromat based synchrotron MAX IV.Journal of synchrotron radiation · 2025Article
- Macromolecular crystallography from an industrial perspective - the impact of synchrotron radiation on structure-based drug discovery.Journal of synchrotron radiation · 2025Article
- Macromolecular crystallography at SPring-8 and SACLA.Journal of synchrotron radiation · 2025Article
- Structural Biology for Target Identification and Validation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Article
- Upgrade of crystallography beamline BL19U1 at the Shanghai Synchrotron Radiation Facility.Journal of applied crystallography · 2024Article
- HEIDI: an experiment-management platform enabling high-throughput fragment and compound screening.Acta crystallographica. Section D, Structural biology · 2024Article
- Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket.Acta crystallographica. Section D, Structural biology · 2024Article
- A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.Nature communications · 2023Article
- Halo Library, a Tool for Rapid Identification of Ligand Binding Sites on Proteins Using Crystallographic Fragment Screening.Journal of medicinal chemistry · 2023Article
- SDU - software for high-throughput automated data collection at the Swiss Light Source.Journal of synchrotron radiation · 2023Article
- Fragment-based drug discovery-the importance of high-quality molecule libraries.Molecular oncology · 2022Review
- Of problems and opportunities-How to treat and how to not treat crystallographic fragment screening data.Protein science : a publication of the Protein Society · 2022Article
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9 authors.
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Abstract
Advances in synchrotron storage rings and beamline automation have pushed data-collection rates to thousands of data sets per week. With this increase in throughput, massive projects such as in-crystal fragment screening have become accessible to a larger number of research groups. The quality of support offered at large-scale facilities allows medicinal chemistry-focused or biochemistry-focused groups to supplement their research with structural biology. Preparing the experiment, analysing multiple data sets and prospecting for interesting complexes of protein and fragments require, for both newcomers and experienced users, efficient management of the project and extensive computational power for data processing and structure refinement. Here, FragMAX, a new complete platform for fragment screening at the BioMAX beamline of the MAX IV Laboratory, is described. The ways in which users are assisted in X-ray-based fragment screenings and in which the fourth-generation storage ring available at the facility is best exploited are also described.
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