ArticleActa crystallographica. Section D, Structural biology2024
Efficient in situ screening of and data collection from microcrystals in crystallization plates.
Article in Acta crystallographica. Section D, Structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A user-friendly goniometer-compatible fixed-target platform for macromolecular crystallography at synchrotrons.Journal of applied crystallography · 2026Article
- Sensing Protein Structural Transitions with Microfluidic Modulation Infrared Spectroscopy.Biosensors · 2025Article
- In situ serial crystallography facilitates 96-well plate structural analysis at low symmetry.IUCrJ · 2024Article
- Managing macromolecular crystallographic data with a laboratory information management system.Acta crystallographica. Section D, Structural biology · 2024Article
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7 authors.
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Abstract
A considerable bottleneck in serial crystallography at XFEL and synchrotron sources is the efficient production of large quantities of homogenous, well diffracting microcrystals. Efficient high-throughput screening of batch-grown microcrystals and the determination of ground-state structures from different conditions is thus of considerable value in the early stages of a project. Here, a highly sample-efficient methodology to measure serial crystallography data from microcrystals by raster scanning within standard in situ 96-well crystallization plates is described. Structures were determined from very small quantities of microcrystal suspension and the results were compared with those from other sample-delivery methods. The analysis of a two-dimensional batch crystallization screen using this method is also described as a useful guide for further optimization and the selection of appropriate conditions for scaling up microcrystallization.
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