ArticleProtein and peptide letters2016
Serial femtosecond crystallography opens new avenues for Structural Biology.
Article in Protein and peptide letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Wavefront sensing at a high-repetition-rate X-ray free-electron laser.Journal of synchrotron radiation · 2026Article
- A phenomenological model of the X-ray pulse statistics of a high-repetition-rate X-ray free-electron laser.IUCrJ · 2023Article
- Anaerobic fixed-target serial crystallography using sandwiched silicon nitride membranes.Acta crystallographica. Section D, Structural biology · 2023Article
- Structural studies of protein-nucleic acid complexes: A brief overview of the selected techniques.Computational and structural biotechnology journal · 2023Review
- Fixed-target serial crystallography at the Structural Biology Center.Journal of synchrotron radiation · 2022Article
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Abstract
Free electron lasers (FELs) provide X-ray pulses in the femtosecond time domain with up to 10(12) higher photon flux than synchrotrons and open new avenues for the determination of difficult to crystallize proteins, like large complexes and human membrane proteins. While the X-ray pulses are so strong that they destroy any solid material, the crystals diffract before they are destroyed. The most successful application of FELs for biology has been the method of serial femtosecond crystallography (SFX) where nano or microcrystals are delivered to the FEL beam in a stream of their mother liquid at room temperature, which ensures the replenishment of the sample before the next X-ray pulse arrives. New injector technology allows also for the delivery of crystal in lipidic cubic phases or agarose, which reduces the sample amounts for an SFX data set by two orders of magnitude. Time-resolved SFX also allows for analysis of the dynamics of biomolecules, the proof of principle being recently shown for light-induced reactions in photosystem II and photoactive yellow protein. An SFX data sets consist of thousands of single crystal snapshots in random orientations, which can be analyzed now "on the fly" by data analysis programs specifically developed for SFX, but de-novo phasing is still a challenge, that might be overcome by two-color experiments or phasing by shape transforms.
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