Source 1review2019Annual Review of Biochemistry
Toolkit/free-electron lasers
free-electron lasers
Also known as: X-ray free-electron lasers
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
very short bursts of X-rays of extremely high intensity that are now accessible as a result of the construction of free-electron lasers, in particular to carry out time-resolved studies of biochemical reactions
Usefulness & Problems
No literature-backed usefulness or problem-fit explainer has been materialized for this record yet.
Published Workflows
Objective: Determine time-ordered structural snapshots of membrane proteins and assemble them into molecular movies to study function.
Why it works: The review states that integrating sample-efficient high-viscosity injectors into pump-probe setups makes it possible to collect whole series of structural snapshots, which can then be assembled into molecular movies.
pump-probe triggering of protein dynamicsserial capture of structural intermediatesX-ray free electron laserstime-resolved serial femtosecond crystallographyhigh-viscosity injectionpump-probe setup integration
Stages
- 1.Integrate high-viscosity injector with pump-probe setup(library_build)
The abstract explicitly states that this integration is what made the downstream time-resolved structural snapshot series possible.
Selection: Establish sample-efficient delivery compatible with pump-probe time-resolved measurements.
- 2.Acquire time-resolved structural snapshot series(functional_characterization)
This is the core measurement stage that produces the ordered structural data needed to study membrane-protein dynamics.
Selection: Determine whole series of structural snapshots by time-resolved serial femtosecond crystallography.
- 3.Assemble structural snapshots into molecular movies(secondary_characterization)
The review presents movie assembly as the step that turns snapshot series into interpretable dynamic models of protein action.
Selection: Combine the structural snapshots into molecular movies of proteins in action.
Steps
- 1.Integrate sample-efficient high-viscosity injectors into pump-probe setupssample-delivery component
Enable sample-efficient time-resolved XFEL measurements.
The abstract explicitly states that this integration is what made the later structural snapshot series possible.
- 2.Determine whole series of structural snapshots by time-resolved serial femtosecond crystallographytime-resolved structural assay
Capture ordered structural states of membrane proteins in action.
This measurement depends on the prior injector and pump-probe integration described in the abstract.
- 3.Assemble structural snapshots into molecular movies of proteins in actionanalysis output
Convert snapshot series into an interpretable dynamic representation of protein function.
Movie assembly follows snapshot acquisition because it uses the collected structural series as its input.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Techniques
Structural CharacterizationTarget processes
No target processes tagged yet.
Input: Chemical
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Free-electron-laser-enabled diffraction techniques support time-resolved studies of biochemical reactions by providing very short, extremely intense X-ray bursts.
very short bursts of X-rays of extremely high intensity that are now accessible as a result of the construction of free-electron lasers, in particular to carry out time-resolved studies of biochemical reactions
Recent advances in mass spectrometry, particularly in combination with other techniques, can generate fundamentally new insights into membrane protein properties and their functional interactions with lipid molecules.
recent advances in mass spectrometry, particularly in combination with other techniques, can generate fundamentally new insights into the properties of membrane proteins and their functional interactions with lipid molecules
Approval Evidence
2 sources3 linked approval claimsfirst-pass slugs free-electron-lasers, x-ray-free-electron-lasers
very short bursts of X-rays of extremely high intensity that are now accessible as a result of the construction of free-electron lasers, in particular to carry out time-resolved studies of biochemical reactions
Source:
Here, I describe recent advances in studying the conformational dynamics of membrane proteins by X-ray free electron lasers.
Source:
review summarysupports
Free-electron-laser-enabled diffraction techniques support time-resolved studies of biochemical reactions by providing very short, extremely intense X-ray bursts.
very short bursts of X-rays of extremely high intensity that are now accessible as a result of the construction of free-electron lasers, in particular to carry out time-resolved studies of biochemical reactions
Source:
review summarysupports
Recent advances in X-ray free electron laser methods have enabled study of membrane-protein conformational dynamics.
Source:
scope statementsupports
The review uses bacteriorhodopsin, photosystem II, and nitric oxide reductase as current study examples for membrane-protein dynamics by XFEL methods.
Source:
Comparisons
No literature-backed comparison notes have been materialized for this record yet.
Ranked Citations
- 1.