ArticleScientific reports2018
Supersaturation-controlled microcrystallization and visualization analysis for serial femtosecond crystallography.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
5 citing papers in PubMed.
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Macromolecular crystallography for mammalian body temperature in support of molecular biophysics methods.Biophysical reviews · 2025Review
- Growing and making nano- and microcrystals.Nature protocols · 2023Review
- Homogeneous batch micro-crystallization of proteins from ammonium sulfate.Acta crystallographica. Section D, Structural biology · 2021Article
- Successful sample preparation for serial crystallography experiments.Journal of applied crystallography · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
20 authors.
Funding
Abstract
Time-resolved serial femtosecond crystallography with X-ray free electron laser (XFEL) holds the potential to view fast reactions occurring at near-physiological temperature. However, production and characterization of homogeneous micron-sized protein crystals at high density remain a bottleneck, due to the lack of the necessary equipments in ordinary laboratories. We describe here supersaturation-controlled microcrystallization and visualization and analysis tools that can be easily used in any laboratory. The microcrystallization conditions of the influenza virus hemagglutinin were initially obtained with low reproducibility, which was improved by employing a rapid evaporation of hanging drops. Supersaturation-controlled microcrystallization was then developed in a vapor diffusion mode, where supersaturation was induced by evaporation in hanging drops sequentially for durations ranging from 30 sec to 3 min, depending on the protein. It was applied successfully to the microcrystal formation of lysozyme, ferritin and hemagglutinin with high density. Moreover, visualization and analysis tools were developed to characterize the microcrystals observed by light microscopy. The size and density distributions of microcrystals analyzed by the tools were found to be consistent with the results of manual analysis, further validated by high-resolution microscopic analyses. Our supersaturation-controlled microcrystallization and visualization and analysis tools will provide universal access to successful XFEL studies.
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Registered trials
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