From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.
Acta Crystallogr D Struct Biol
; 80(Pt 2): 60-79, 2024 Feb 01.
Article
in En
| MEDLINE
| ID: mdl-38265875
ABSTRACT
Over the last decade, the development of time-resolved serial crystallography (TR-SX) at X-ray free-electron lasers (XFELs) and synchrotrons has allowed researchers to study phenomena occurring in proteins on the femtosecond-to-minute timescale, taking advantage of many technical and methodological breakthroughs. Protein crystals of various sizes are presented to the X-ray beam in either a static or a moving medium. Photoactive proteins were naturally the initial systems to be studied in TR-SX experiments using pump-probe schemes, where the pump is a pulse of visible light. Other reaction initiations through small-molecule diffusion are gaining momentum. Here, selected examples of XFEL and synchrotron time-resolved crystallography studies will be used to highlight the specificities of the various instruments and methods with respect to time resolution, and are compared with cryo-trapping studies.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Proteins
/
Synchrotrons
Language:
En
Journal:
Acta Crystallogr D Struct Biol
Year:
2024
Document type:
Article
Affiliation country:
Francia