ArticleIUCrJ2014
Room-temperature macromolecular serial crystallography using synchrotron radiation.
Article in IUCrJ, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.
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Who cites it
156 citing papers in PubMed.
- Biological applications at the AQUA beamline of the EuPRAXIA@SPARC_LAB free electron laser.European biophysics journal : EBJ · 2026Article
- Automated microbatch-under-oil phase diagrams to rationalize serial crystallography sample preparation.IUCrJ · 2026Article
- Article
- 50th anniversary of the Stanford SSRL synchrotron radiation and protein crystallography initiative.Journal of synchrotron radiation · 2026Article
- A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026Review
- Spitrobot-2 advances time-resolved cryo-trapping crystallography to under 25 ms.Communications chemistry · 2025Article
- Sample delivery methods for protein X-ray crystallography with a special focus on sample consumption.Nature communications · 2025Review
- Standard Sample Preparation for Serial Femtosecond Crystallography.Biomolecules · 2025Review
- Evolution of macromolecular crystallography beamlines at the Swiss Light Source and SwissFEL.Journal of synchrotron radiation · 2025Article
- Combining MicroED and native mass spectrometry for structural discovery of enzyme-small molecule complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Review
- Protein crystallization and structure determination at room temperature in the CrystalChip.FEBS open bio · 2025Article
- Unit-cell parameters determination from a set of independent electron diffraction zonal patterns.Acta crystallographica. Section A, Foundations and advances · 2025Article
- Present and future structural biology activities at DESY and the European XFEL.Journal of synchrotron radiation · 2025Article
- Combining MicroED and native mass spectrometry for structural discovery of enzyme-biosynthetic inhibitor complexes.bioRxiv : the preprint server for biology · 2025Article
- Article
- Exploiting fourth-generation synchrotron radiation for enzyme and photoreceptor characterization.IUCrJ · 2025Article
- Useful experimental aspects of small-wedge synchrotron crystallography for accurate structure analysis of protein molecules.Acta crystallographica. Section D, Structural biology · 2025Article
- Scaling and merging time-resolved pink-beam diffraction with variational inference.Structural dynamics (Melville, N.Y.) · 2024Article
96 more citing papers are in PubMed but not listed here.
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20 authors.
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Abstract
A new approach for collecting data from many hundreds of thousands of microcrystals using X-ray pulses from a free-electron laser has recently been developed. Referred to as serial crystallography, diffraction patterns are recorded at a constant rate as a suspension of protein crystals flows across the path of an X-ray beam. Events that by chance contain single-crystal diffraction patterns are retained, then indexed and merged to form a three-dimensional set of reflection intensities for structure determination. This approach relies upon several innovations: an intense X-ray beam; a fast detector system; a means to rapidly flow a suspension of crystals across the X-ray beam; and the computational infrastructure to process the large volume of data. Originally conceived for radiation-damage-free measurements with ultrafast X-ray pulses, the same methods can be employed with synchrotron radiation. As in powder diffraction, the averaging of thousands of observations per Bragg peak may improve the ratio of signal to noise of low-dose exposures. Here, it is shown that this paradigm can be implemented for room-temperature data collection using synchrotron radiation and exposure times of less than 3 ms. Using lysozyme microcrystals as a model system, over 40 000 single-crystal diffraction patterns were obtained and merged to produce a structural model that could be refined to 2.1 Å resolution. The resulting electron density is in excellent agreement with that obtained using standard X-ray data collection techniques. With further improvements the method is well suited for even shorter exposures at future and upgraded synchrotron radiation facilities that may deliver beams with 1000 times higher brightness than they currently produce.
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