ArticleActa crystallographica. Section D, Structural biology2019
Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments.
Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed.
- A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons.Journal of applied crystallography · 2026Article
- Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.Nature communications · 2025Article
- Real-time analysis of nanoscale dynamics in membrane protein insertion via single-molecule imaging.Biophysics reports · 2024Article
- Photoswitch dissociation from a G protein-coupled receptor resolved by time-resolved serial crystallography.Nature communications · 2024Article
- Characterization and evaluation of photolabile (µ-peroxo)(µ-hydroxo)bis[bis(bipyridyl)cobalt caged oxygen compounds to facilitate time-resolved crystallographic studies of cytochrome c oxidase.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024Article
- Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochromeScience advances · 2023Article
- A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography.Journal of applied crystallography · 2023Article
- A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography.Journal of applied crystallography · 2023Article
- Serial femtosecond crystallography.Nature reviews. Methods primers · 2022Article
- Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre.Acta crystallographica. Section D, Structural biology · 2022Article
- Novel combined crystallization plate for high-throughput crystal screening and in situ data collection at a crystallography beamline.Acta crystallographica. Section F, Structural biology communications · 2021Article
- BioMAX - the first macromolecular crystallography beamline at MAX IV Laboratory.Journal of synchrotron radiation · 2020Article
- Current status and future opportunities for serial crystallography at MAX IV Laboratory.Journal of synchrotron radiation · 2020Article
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16 authors.
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Abstract
Serial crystallography is having an increasing impact on structural biology. This emerging technique opens up new possibilities for studying protein structures at room temperature and investigating structural dynamics using time-resolved X-ray diffraction. A limitation of the method is the intrinsic need for large quantities of well ordered micrometre-sized crystals. Here, a method is presented to screen for conditions that produce microcrystals of membrane proteins in the lipidic cubic phase using a well-based crystallization approach. A key advantage over earlier approaches is that the progress of crystal formation can be easily monitored without interrupting the crystallization process. In addition, the protocol can be scaled up to efficiently produce large quantities of crystals for serial crystallography experiments. Using the well-based crystallization methodology, novel conditions for the growth of showers of microcrystals of three different membrane proteins have been developed. Diffraction data are also presented from the first user serial crystallography experiment performed at MAX IV Laboratory.
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