ArticleNature communications2023
A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Convolvulus althaeoides as a Potential Natural Source in Cancer Prophylaxis and Treatment: LC-ESI-MS/MS, GC-MS, In Vitro, and In Silico Investigations.Chemistry & biodiversity · 2026Article
- Elucidating the Covalent Binding of Ottelione A and Withaferin A at the Colchicine Site of β‑Tubulin.ACS omega · 2026Article
- PEO-sheathed liquid jets increase sample delivery stability for serial femtosecond X-ray crystallography.Scientific reports · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification.bioRxiv : the preprint server for biology · 2025Article
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Room-temperature X-ray fragment screening with serial crystallography.Nature communications · 2025Article
- Advancing macromolecular structure determination with microsecond X-ray pulses at a 4th generation synchrotron.Communications chemistry · 2025Article
- A snapshot love story: what serial crystallography has done and will do for us.Acta crystallographica. Section D, Structural biology · 2024Review
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
Corrections and comments
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Authors and funding
30 authors.
Funding
Abstract
Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced. In-built temperature control of samples facilitated optimal extrusion and supported sample stability. After commissioning the device with lysozyme crystals, we collected time-resolved data using crystals of a membrane-bound, light-driven sodium pump. Static data were also collected from the soluble protein tubulin that was soaked with a series of small molecule drugs. Using these data, we identify low occupancy (as little as 30%) ligands using a minimal amount of data from a serial crystallography experiment, a result that could be exploited for structure-based drug design.
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