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Serial femtosecond X-ray diffraction of 30S ribosomal subunit microcrystals in liquid suspension at ambient temperature using an X-ray free-electron laser
- Source :
- Acta crystallographica / F 69(9), 1066-1069 (2013). doi:10.1107/S174430911302099X, Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Publication Year :
- 2013
- Publisher :
- Blackwell, 2013.
-
Abstract
- Serial femtosecond X-ray (SFX) diffraction extending beyond 6 Å resolution using T. thermophilus 30S ribosomal subunit crystals is reported.<br />High-resolution ribosome structures determined by X-ray crystallography have provided important insights into the mechanism of translation. Such studies have thus far relied on large ribosome crystals kept at cryogenic temperatures to reduce radiation damage. Here, the application of serial femtosecond X-ray crystallography (SFX) using an X-ray free-electron laser (XFEL) to obtain diffraction data from ribosome microcrystals in liquid suspension at ambient temperature is described. 30S ribosomal subunit microcrystals diffracted to beyond 6 Å resolution, demonstrating the feasibility of using SFX for ribosome structural studies. The ability to collect diffraction data at near-physiological temperatures promises to provide fundamental insights into the structural dynamics of the ribosome and its functional complexes.
- Subjects :
- Diffraction
Biophysics
Analytical chemistry
Electrons
Ribosome Subunits, Small, Bacterial
Crystallography, X-Ray
Biochemistry
law.invention
X-Ray Diffraction
Structural Biology
law
Genetics
30S
ddc:530
Chemistry
Lasers
Thermus thermophilus
Laboratory Communications
serial femtosecond X-ray crystallography
Resolution (electron density)
Temperature
X-ray
Translation (biology)
Condensed Matter Physics
Laser
enzymes and coenzymes (carbohydrates)
Crystallography
ribosome
30S ribosomal subunit
X-ray crystallography
Femtosecond
bacteria
X-ray free-electron laser
Crystallization
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica / F 69(9), 1066-1069 (2013). doi:10.1107/S174430911302099X, Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- Accession number :
- edsair.doi.dedup.....684c66b38bdd6d9b1d47a6218c191fe4