ArticleIUCrJ2019
High-throughput structures of protein-ligand complexes at room temperature using serial femtosecond crystallography.
Article in IUCrJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- A simple and practical approach for protein serial crystallography using grease matrix and large-area support film.Journal of synchrotron radiation · 2026Article
- Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography.IUCrJ · 2026Article
- Cefdinir binding to a class A β-lactamase revealed by serial cryo-crystallography.Acta crystallographica. Section D, Structural biology · 2026Article
- Microfluidic Devices for High-Throughput In Situ Serial Crystallography.Advances in biochemical engineering/biotechnology · 2026Review
- Binding mode of Isoxazolyl Penicillins to a Class-A β-lactamase at ambient conditions.Communications chemistry · 2025Article
- Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.Communications chemistry · 2025Article
- In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.IUCrJ · 2024Article
- Efficient in situ screening of and data collection from microcrystals in crystallization plates.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
- Micro-structured polymer fixed targets for serial crystallography at synchrotrons and XFELs.IUCrJ · 2023Article
- A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography.Journal of applied crystallography · 2023Article
- Room-temperature crystallography reveals altered binding of small-molecule fragments to PTP1B.eLife · 2023Article
- Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches.Frontiers in molecular biosciences · 2023Article
- Sample Preparation for Time-Resolved Serial Crystallography: Practical Considerations.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Room-temperature serial synchrotron crystallography of the human phosphatase PTP1B.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Article
- A new strategy for hit generation: Novel in cellulo active inhibitors of CYP121A1 from Mycobacterium tuberculosis via a combined X-ray crystallographic and phenotypic screening approach (XP screen).European journal of medicinal chemistry · 2022Article
- Experiences From Developing Software for Large X-Ray Crystallography-Driven Protein-Ligand Studies.Frontiers in molecular biosciences · 2022Article
- Best practices for time-resolved serial synchrotron crystallography.Acta crystallographica. Section D, Structural biology · 2022Review
- Spectral monitoring at SwissFEL using a high-resolution on-line hard X-ray single-shot spectrometer.Journal of synchrotron radiation · 2021Article
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
High-throughput X-ray crystal structures of protein-ligand complexes are critical to pharmaceutical drug development. However, cryocooling of crystals and X-ray radiation damage may distort the observed ligand binding. Serial femtosecond crystallography (SFX) using X-ray free-electron lasers (XFELs) can produce radiation-damage-free room-temperature structures. Ligand-binding studies using SFX have received only modest attention, partly owing to limited beamtime availability and the large quantity of sample that is required per structure determination. Here, a high-throughput approach to determine room-temperature damage-free structures with excellent sample and time efficiency is demonstrated, allowing complexes to be characterized rapidly and without prohibitive sample requirements. This yields high-quality difference density maps allowing unambiguous ligand placement. Crucially, it is demonstrated that ligands similar in size or smaller than those used in fragment-based drug design may be clearly identified in data sets obtained from <1000 diffraction images. This efficiency in both sample and XFEL beamtime opens the door to true high-throughput screening of protein-ligand complexes using SFX.
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