Serial femtosecond crystallography: the first five years

Protein crystallography using synchrotron radiation sources has had a tremendous impact on biology, having yielded the structures of thousands of proteins and given detailed insight into their mechanisms. However, the technique is limited by the requirement for macroscopic crystals, which can be dif...

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Bibliographic Details
Published in:IUCrJ Vol. 2; no. 2; pp. 246 - 255
Main Author: Schlichting, Ilme
Format: Journal Article
Language:English
Published: England International Union of Crystallography 01.03.2015
Subjects:
Crystal structure
Crystallography
Crystals
Diffraction
Exposure
FELs
Femtosecond
microcrystals
Protein research
Proteins
Radiation damage
serial femtosecond crystallography
SFX
Structure
Synchrotron radiation
time-resolved crystallography
X-ray lasers
SFX
radiation damage
FELs
X-ray lasers
microcrystals
serial femtosecond crystallography
time-resolved crystallography
ISSN:2052-2525, 2052-2525
Online Access:Get full text
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Summary:Protein crystallography using synchrotron radiation sources has had a tremendous impact on biology, having yielded the structures of thousands of proteins and given detailed insight into their mechanisms. However, the technique is limited by the requirement for macroscopic crystals, which can be difficult to obtain, as well as by the often severe radiation damage caused in diffraction experiments, in particular when using tiny crystals. To slow radiation damage, data collection is typically performed at cryogenic temperatures. With the advent of free-electron lasers (FELs) capable of delivering extremely intense femtosecond X-ray pulses, this situation appears to be remedied, allowing the structure determination of undamaged macromolecules using either macroscopic or microscopic crystals. The latter are exposed to the FEL beam in random orientations and their diffraction data are collected at cryogenic or room temperature in a serial fashion, since each crystal is destroyed upon a single exposure. The new approaches required for crystal growth and delivery, and for diffraction data analysis, including de novo phasing, are reviewed. The opportunities and challenges of SFX are described, including applications such as time-resolved measurements and the analysis of radiation damage-prone systems.
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ISSN:2052-2525
2052-2525
DOI:10.1107/S205225251402702X