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Photon sources, such as table-top lasers, synchrotron X-rays and free-electron lasers (FELs), can be used to explore and understand the structure of materials through photon-matter interactions. Short wavelength and coherent photons generated, when relativistic electrons travel through undulator, from FELs are tunable and compressible to few femtosecond pulses to take snapshots of structures in order to study the time-dependent interactions and dynamics of different materials. These facilities are becoming increasingly popular in diverse research fields, because of their tunability and high spatial and temporal resolution.
In this collection, we showcase recent articles published in Nature Communications on FEL generation and characterization and their application in fundamental studies of light-matter interaction. These research papers include FEL instrumentation and techniques, investigations on photoionization and ultrafast processes in atomic and molecular physics, chemical and physical properties of condensed matter systems, and probing of structure and dynamics of biological samples. This collection highlights the increasingly significant role FELs are having on research across a diverse range of subject areas and Nature Communications’ role as a suitable platform in publishing such multidisciplinary works.
X-ray free electron lasers are increasingly available for use in macromolecular structure determination. Here, the authors describe the successful use of selenium single-wavelength anomalous diffraction data to calculate experimentally derived phases.
Mass spectrometry is a leading method used for sequencing peptides and proteins by fragmentation followed by analysis of the sequence fragments. Here, the authors use infrared spectroscopy to characterize the structures of peptide fragments formed during electron transfer dissociation.
Diacylglycerol kinase is a small bacterial membrane-bound trimer that catalyses diacylglycerol conversion to phosphatidic acid. Here, the authors solve the crystal structure of the kinase bound to a lipid substrate and an ATP analogue, and show that the active site arose through convergent evolution.
Smoothened receptors (SMO) play a key role in the Hedgehog signalling pathway. Here the authors present the structure of a multi-domain human SMO with a rationally designed stabilizing ligand bound in the transmembrane domain of the receptor, and propose a model for SMO activation.
Imaging live cells at nanometre resolution is challenging because radiation damage kills the cells during exposure. Here, the authors overcome this difficulty in a ‘diffraction before destruction’ experiment using an X-ray laser and record signal to 4 nm resolution on a free-flying cell.
Structure determination of glycosylated HIV-1 envelope (Env) trimers complexed with broadly neutralizing antibodies (bNAbs) promotes a better understanding of bNAb epitopes. Here the authors present the structures of natively-glycosylated Env in complex with the highly-potent bNAb BG18, which is of interest for HIV-1 vaccine development.
Serial femtosecond crystallography and the use of X-ray free-electron lasers (XFEL) promise to revolutionize structural biology. Here, the authors describe refinements that reduce the redundancy required to obtain quality XFEL data and report a 1.75-Å structure—not obtainable by synchrotron radiation—using less than 6,000 crystals.
Using photosensitive caged-compound for femtosecond crystallography at X-ray free electron lasers would allow the structure determination of reaction intermediates. Here the authors demonstrate the feasibility of this approach with a caged NO-compound and present the initial NO-bound intermediate structure of cytochrome P450 nitric oxide reductase.
The structures of amyloid fibres are currently primarily studied through solid state NMR and cryo-EM. Here the authors present a free-standing graphene support device that allows diffraction imaging of non-crystalline amyloid fibrils with single X-ray pulses from an X-ray free-electron laser.
Localized chemical events such as the breakage of a bond between a protein and a ligand may trigger a global protein conformational change. Here, the authors use an X-ray free-electron laser to track the motion of myoglobin in response to photoinduced ligand release, and observe a picosecond proteinquake.
Serial femtosecond crystallography using X-ray free-electron lasers has huge potential for time-resolved structural experiments. Here, the authors present a structure of the light-driven proton pump bacteriorhodopsin using these techniques.
The new European X-Ray Free-Electron Laser (EuXFEL) is the first XFEL that generates X-ray pulses with a megahertz inter-pulse spacing. Here the authors demonstrate that high-quality and damage-free protein structures can be obtained with the currently available 1.1 MHz repetition rate pulses using lysozyme as a test case and furthermore present a β-lactamase structure.
X-ray free-electron lasers produce bright femtosecond X-ray pulses. Here, the authors use a two-colour X-ray free-electron laser beam for simultaneous two-wavelength data collection and show that protein structures can be determined with multiple wavelength anomalous dispersion phasing, which is important for difficult-to-phase projects.
The European X-ray free-electron laser (EuXFEL) in Hamburg is the first megahertz (MHz) repetition rate XFEL. Here the authors use lysozyme crystals and microcrystals from jack bean proteins and demonstrate that damage-free high quality data can be collected at a MHz repetition rate.