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- W2738632497 abstract "XFELs allow radiation damage to be overcome, enabling the determination of high-resolution room-temperature structures of difficult-to-crystallize proteins, for which only small crystals are available, and of extremely radiation-sensitive macromolecules, such as metalloenzymes. De novo phasing at XFELs has been established on several different targets and by different methods, thereby enabling the determination of the structure of novel macromolecules of biological interest. The extremely short fs duration of XFEL pulses provides access to dynamic information about unstable intermediate states and irreversible reactions. The development of new injectors, crystal delivery media, and fixed target devices has dramatically reduced the amount of required crystallized protein. Mixing injectors provide an important avenue to study biological interactions in 4D space. Developments in data-processing software have reduced the required amount of data and improved data quality. X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle. Intense fs XFEL pulses enable high-resolution room-temperature structure determination of difficult-to-crystallize biological macromolecules, while simultaneously opening a new era of time-resolved structural studies. Here, we review the latest developments in instrumentation, sample delivery, data analysis, crystallization methods, and applications of SFX to important biological questions, and conclude with brief insights into the bright future of structural biology using XFELs. X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular structural biology due to the unique combination of spatial coherence, extreme peak brilliance, and short duration of X-ray pulses. A recently emerged serial femtosecond (fs) crystallography (SFX) approach using XFEL radiation overcomes some of the biggest hurdles of traditional crystallography related to radiation damage through the diffraction-before-destruction principle. Intense fs XFEL pulses enable high-resolution room-temperature structure determination of difficult-to-crystallize biological macromolecules, while simultaneously opening a new era of time-resolved structural studies. Here, we review the latest developments in instrumentation, sample delivery, data analysis, crystallization methods, and applications of SFX to important biological questions, and conclude with brief insights into the bright future of structural biology using XFELs. cryo-cooling crystals during crystallographic data collection to reduce radiation damage effects. the ratio between the number of detector images with identified diffraction spots and the total number of collected images. experimental approaches for deriving phases of structure factors from measured intensities using methods such as single/multiple isomorphous replacement (SIR/MIR), single/multiple-wavelength anomalous dispersion (SAD/MAD) or single/multiple isomorphous replacement combined with anomalous scattering (SIRAS/MIRAS). a concept for sample delivery that relies on immobilizing the sample on a solid support for serial data collection by rastering with the XFEL beam. a device used to position the crystal in selected orientations for optimization of data collection. a gel-like membrane mimetic matrix that supports membrane protein crystallization from a native-like environment and can be used for efficient sample delivery. a synchrotron beamline equipped with beam-focusing optics and precise goniometers to enable data collection from micrometer-sized crystals. a method for solving the phase problem (see below) by using initial phases from a similar (homologous) protein. reconstitution of electron density requires the knowledge of structure factor phases; however, in a crystallographic experiment, only structure factor amplitudes, but not their phases, are measured. a time-resolved experiment in which an optical pulse (pump) triggers a reaction followed by an XFEL pulse (probe) at a variable time delay. primary radiation damage implies immediate ionization effects caused by absorbed photons and ejected photoelectrons, while secondary radiation damage occurs through (mainly) the formation of free radicals (caused by primary ionization events). a measure of the visibility of details in a density map. In crystallography, resolution is traditionally measured in Ångströms (1 Å = 0.1 nm). The lower the value, the more details can be seen. At approximately 3.5 Å, individual amino acid side chains are visible and at 2.5 Å, waters are discernible, at better than 2 Å resolution, multiple amino acid conformations could be modeled. a process by which a laser beam is generated from a high-energy electron beam. An electron bunch is accelerated to a relativistic speed and passed through a long undulator, which supplies a transverse magnetic field that is periodically changing in space, encouraging electrons to follow a sinusoidal path emitting X-ray photons. Interaction between spontaneously emitted photons and electrons induces alignment of electrons (‘microbunching’), thereby causing them to emit X-ray radiation coherently. a data collection paradigm where diffraction data are collected from a large number of microcrystals in a ‘one crystal, one shot’ approach using an XFEL. a synchrotron source equipped with straight sections containing undulator or wiggler magnets leading to increased brilliance as well as spatial and temporal coherence of X-ray beams compared with earlier-generation synchrotron sources. a method used to visualize conformational transitions occurring within a protein as it performs its function with a high spatial and temporal resolution. The time component is achieved by collecting X-ray data at several time points after initiation of the reaction. a latest-generation light source producing ultrabright pulses of coherent X-rays with ultrashort duration using the SASE principle on freely moving electrons." @default.
- W2738632497 created "2017-07-31" @default.
- W2738632497 creator A5031507797 @default.
- W2738632497 creator A5057336284 @default.
- W2738632497 creator A5058112118 @default.
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- W2738632497 date "2017-09-01" @default.
- W2738632497 modified "2023-10-15" @default.
- W2738632497 title "A Bright Future for Serial Femtosecond Crystallography with XFELs" @default.
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