ReviewArchives of biochemistry and biophysics2016
Serial femtosecond crystallography: A revolution in structural biology.
Review in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
60 citing papers in PubMed.
- Perspectives for pharmaceutical screening at XFEL sources using the example of Lassa virus endonuclease.Acta crystallographica. Section D, Structural biology · 2026Article
- Advances of 3D microcrystals electron diffraction for transmembrane protein structure determination.Biophysical journal · 2026Review
- Plant structural biology: Emerging technologies and future biological insights.The Plant journal : for cell and molecular biology · 2026Review
- Microfluidic Devices for High-Throughput In Situ Serial Crystallography.Advances in biochemical engineering/biotechnology · 2026Review
- Strategies for mitigating radiation damage and improving data completeness in 3D electron diffraction of protein crystals.Acta crystallographica. Section D, Structural biology · 2026Article
- Structural insights into full-length human fascin1: a target for cancer treatment.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Spontaneous base flipping helps drive Nsp15's preferences in double stranded RNA substrates.Nature communications · 2025Article
- Effect of crystal-to-detector distance shift on data processing in serial crystallography.PloS one · 2025Article
- Recent Advances in Omics, Computational Models, and Advanced Screening Methods for Drug Safety and Efficacy.Toxics · 2024Review
- Innovative Strategies in X-ray Crystallography for Exploring Structural Dynamics and Reaction Mechanisms in Metabolic Disorders.Journal of personalized medicine · 2024Review
- Review
- FLEXR: automated multi-conformer model building using electron-density map sampling.Acta crystallographica. Section D, Structural biology · 2023Article
- Evaluating the impact of X-ray damage on conformational heterogeneity in room-temperature (277 K) and cryo-cooled protein crystals.Acta crystallographica. Section D, Structural biology · 2022Article
- Resolving the interlayer distance of cationic pyrene clusters embedded in superfluid helium droplets using electron diffraction.The Journal of chemical physics · 2022Article
- Co-flow injection for serial crystallography at X-ray free-electron lasers.Journal of applied crystallography · 2022Article
- Beef tallow injection matrix for serial crystallography.Scientific reports · 2022Article
- Molecular dynamics analysis of biomolecular systems including nucleic acids.Biophysics and physicobiology · 2022Article
- Near-physiological-temperature serial crystallography reveals conformations of SARS-CoV-2 main protease active site for improved drug repurposing.Structure (London, England : 1993) · 2021Article
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- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Macromolecular crystallography at synchrotron sources has proven to be the most influential method within structural biology, producing thousands of structures since its inception. While its utility has been instrumental in progressing our knowledge of structures of molecules, it suffers from limitations such as the need for large, well-diffracting crystals, and radiation damage that can hamper native structural determination. The recent advent of X-ray free electron lasers (XFELs) and their implementation in the emerging field of serial femtosecond crystallography (SFX) has given rise to a remarkable expansion upon existing crystallographic constraints, allowing structural biologists access to previously restricted scientific territory. SFX relies on exceptionally brilliant, micro-focused X-ray pulses, which are femtoseconds in duration, to probe nano/micrometer sized crystals in a serial fashion. This results in data sets comprised of individual snapshots, each capturing Bragg diffraction of single crystals in random orientations prior to their subsequent destruction. Thus structural elucidation while avoiding radiation damage, even at room temperature, can now be achieved. This emerging field has cultivated new methods for nanocrystallogenesis, sample delivery, and data processing. Opportunities and challenges within SFX are reviewed herein.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.