Source 1review2022Current Opinion in Structural Biology
Toolkit/time-resolved serial oscillation crystallography
time-resolved serial oscillation crystallography
Also known as: serial oscillation crystallography, time-resolved crystallography, XFEL time-resolved crystallography
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Time-resolved serial oscillation crystallography is a synchrotron-based, room-temperature X-ray diffraction method that collects, processes, and merges monochromatic oscillation data from fewer than 100 crystals. It was used to follow light-driven structural changes in a blue-light photoreceptor domain with 63 ms time resolution and to visualize time-dependent rearrangements of both the protein and its chromophore.
Usefulness & Problems
Why this is useful
This method is useful for capturing structural dynamics of light-triggered protein reactions at room temperature while reducing crystal consumption to fewer than 100 samples. It provides time-series diffraction snapshots that reveal the buildup of photoreaction intermediates and associated conformational changes in both protein and chromophore.
Problem solved
It addresses the challenge of observing millisecond structural transitions during photoconversion using synchrotron X-ray crystallography under room-temperature conditions. The reported implementation also reduces the sample burden relative to serial approaches by enabling analysis from fewer than 100 crystals.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
light-triggered photoconversionlight-triggered photoconversiontime-resolved serial x-ray diffraction snapshottingtime-resolved serial x-ray diffraction snapshottingTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
application domain: light-sensitive proteinscofactor dependency: cofactor requirement unknownimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementmethod scope: mechanistic crystallographymodality: experimentaloperating role: sensorroom temperature: Truesample count text: <100 samplestime resolution ms: 63time resolved: Trueuses reaction in crystal: Trueuses synchrotron: True
The method uses synchrotron-based monochromatic X-ray oscillation diffraction at room temperature and a light input to trigger photoconversion. The available evidence indicates serial data collection with processing and merging across fewer than 100 crystals, but it does not specify construct design, illumination wavelength, crystal delivery format, or software workflow.
The supplied evidence describes application to a single blue-light photoreceptor domain and does not establish performance across other proteins, triggers, or timescales. The evidence also does not report broader benchmarking, independent replication, or practical details such as beamline requirements, data-processing constraints, or limits on reaction reversibility and crystal tolerance.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2009Crystallography Reviews
Source 3primary paper2020IUCrJ
Ranked Claims
Structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.
The structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.
Recent progress has combined time-resolved crystallography at X-ray free electron lasers with quantum chemical calculations to study structural changes in light-sensitive proteins following photoexcitation.
Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
time resolution 63 ms
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
time resolution 63 ms
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
time resolution 63 ms
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
time resolution 63 ms
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
time resolution 63 ms
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
sample count 100 samples
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
sample count 100 samples
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
sample count 100 samples
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
sample count 100 samples
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
sample count 100 samples
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
Kinetic crystallography enables crystallography to address protein mechanism by initiating biological turnover in crystals and observing transient structural species.
UV/visible single-crystal spectroscopy is essential for designing, interpreting, and validating kinetic crystallography experiments.
Approval Evidence
3 sources7 linked approval claimsfirst-pass slugs kinetic-crystallography, time-resolved-crystallography-at-x-ray-free-electron-lasers, time-resolved-serial-oscillation-crystallography
Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.
Source:
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
Source:
By initiating biological turnover in the crystal, transient structural species form, which may be filmed 'on the fly' by Laue diffraction or captured by trapping methods. These strategies are jointly referred to as 'kinetic crystallography'.
Source:
capability summarysupports
Structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.
The structural dynamics underlying molecular mechanisms of light-sensitive proteins can be studied by a variety of experimental and computational biophysical techniques.
Source:
review scope summarysupports
Recent progress has combined time-resolved crystallography at X-ray free electron lasers with quantum chemical calculations to study structural changes in light-sensitive proteins following photoexcitation.
Here we review recent progress in combining time-resolved crystallography at X-ray free electron lasers and quantum chemical calculations to study structural changes in photoenzymes, photosynthetic proteins, photoreceptors, and photoswitchable fluorescent proteins following photoexcitation.
Source:
application resultsupports
Using the reported method, the authors monitored with 63 ms time resolution the progressive photoconversion of a blue-light photoreceptor domain in a crystal from the dark to the light state.
Using this method, we monitored with a time resolution of 63 ms how the population of a blue-light photoreceptor domain in a crystal progressively photoconverts from the dark to the light state.
Source:
method capabilitysupports
The reported method enables room-temperature collection, processing and merging of X-ray oscillation diffraction data from fewer than 100 samples to observe buildup of a photoreaction intermediate species.
A method is reported here, using monochromatic synchrotron radiation, for the room-temperature collection, processing and merging of X-ray oscillation diffraction data from <100 samples in order to observe the build up of a photoreaction intermediate species.
Source:
structural insightsupports
The resulting time series of snapshots allows detailed visualization of gradual rearrangement of both the protein and chromophore during photoconversion.
The series of resulting snapshots allows us to visualize in detail the gradual rearrangement of both the protein and chromophore during this process.
Source:
method capabilitysupports
Kinetic crystallography enables crystallography to address protein mechanism by initiating biological turnover in crystals and observing transient structural species.
Source:
method dependencysupports
UV/visible single-crystal spectroscopy is essential for designing, interpreting, and validating kinetic crystallography experiments.
Source:
Comparisons
Source-backed strengths
The method achieved 63 ms time resolution for monitoring progressive photoconversion of a blue-light photoreceptor domain from dark to light state. It enabled collection, processing, and merging of monochromatic oscillation diffraction data from fewer than 100 samples and produced a time series that visualized gradual rearrangements of the protein and chromophore.
Ranked Citations
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