| Home > Publications database > Virus Structures by X-Ray Free-Electron Lasers |
| Journal Article | PUBDB-2019-03664 |
;
2019
Annual Reviews
Palo Alto, Calif.
This record in other databases:
Please use a persistent id in citations: doi:10.1146/annurev-virology-092818-015724
Abstract: Until recently X-ray crystallography has been the standard technique forvirus structure determinations. Available X-ray sources have continuouslyimproved over the decades, leading to the realization of X-ray free-electronlasers (XFELs). They provide high-intensity femtosecond X-ray pulses,which allow for new kinds of experiments by making use of the diffractionbefore-destruction principle. By overcoming classical dose constraints, theyat least in principle allow researchers to perform X-ray virus structuredetermination for single particles at room temperature. Simultaneously,the availability of XFELs led to the development of the method of serialfemtosecond crystallography, where a crystal structure is determined fromthe measurement of hundreds to thousands of microcrystals. In the case ofvirus crystallography this method does not require freezing of the crystalsand allows researchers to perform experiments under non-equilibriumconditions (e.g., by laser-induced temperature jumps or rapid chemicalmixing), which is currently not possible with electron microscopy.
|
The record appears in these collections: |