ArticleStructural dynamics (Melville, N.Y.)2019
A shared vision for macromolecular crystallography over the next five years.
Article in Structural dynamics (Melville, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine.Biomolecules · 2025Review
- EIGER2 hybrid-photon-counting X-ray detectors for advanced synchrotron diffraction experiments.Journal of synchrotron radiation · 2023Article
- Data collection from crystals grown in microfluidic droplets.Acta crystallographica. Section D, Structural biology · 2022Article
- Experiences From Developing Software for Large X-Ray Crystallography-Driven Protein-Ligand Studies.Frontiers in molecular biosciences · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- 'International journal of molecular sciences · 2021Article
- IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition.Acta crystallographica. Section D, Structural biology · 2021Article
- Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Multi-crystal data collection using synchrotron radiation as exemplified with low-symmetry crystals of Dps.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Pre-clustering data sets using cluster4x improves the signal-to-noise ratio of high-throughput crystallography drug-screening analysis.Acta crystallographica. Section D, Structural biology · 2020Article
- Transactions from the 69th Annual Meeting of the American Crystallographic Association: Data best practices-current state and future needs.Structural dynamics (Melville, N.Y.) · 2020Review
- Protein X-ray Crystallography and Drug Discovery.Molecules (Basel, Switzerland) · 2020Review
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Authors and funding
2 authors.
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Abstract
Macromolecular crystallography (MX) is the dominant means of determining the three-dimensional structures of biological macromolecules, but the method has reached a critical juncture. New diffraction-limited storage rings and upgrades to the existing sources will provide beamlines with higher flux and brilliance, and even the largest detectors can collect at rates of several hundred hertz. Electron cryomicroscopy is successfully competing for structural biologists' most exciting projects. As a result, formerly scarce beam time is becoming increasingly abundant, and beamlines must innovate to attract users and ensure continued funding. Here, we will show how data collection has changed over the preceding five years and how alternative methods have emerged. We then explore how MX at synchrotrons might develop over the next five years. We predict that, despite the continued dominance of rotation crystallography, applications previously considered niche or experimental, such as serial crystallography, pink-beam crystallography, and crystallography at energies above 25 keV and below 5 keV, will rise in prominence as beamlines specialize to offer users the best value. Most of these emerging methods will require new hardware and software. With these advances, MX will more efficiently provide the high-resolution structures needed for drug development. MX will also be able to address a broader range of questions than before and contribute to a deeper understanding of biological processes in the context of integrative structural biology.
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