Abstract
With time-resolved crystallography (TRX), it is possible to follow the reaction dynamics in biological macromolecules by investigating the structure of transient states along the reaction coordinate. X-ray free electron lasers (XFELs) have enabled TRX experiments on previously uncharted femtosecond timescales. Here, we review the recent developments, opportunities, and challenges of pump-probe TRX at XFELs.
Highlights
The chemical reactions that enable life are catalyzed by proteins
Physical or chemical trapping [4,5] methods work by artificially prolonging the lifetime of reaction intermediates so that their structures can be determined with conventional crystallography
time-resolvedX-ray crystallography (TRX) experiments with a time resolution up to 100 ps can be performed with synchrotron X-ray sources while X-ray free electron lasers (XFELs) are available to probe shorter time scales
Summary
The chemical reactions that enable life are catalyzed by proteins. Proteins change their structures while they perform these functions. After an adjustable time-delay (∆t), the crystals are illuminated by an X-ray pulse, known as the “probe” pulse, which generates a diffraction pattern This is called a pump-probe experiment (Figure 1). Time-Resolved Crystallography at Synchrotron Sources an optical laser pulse (red bar) initiates the reaction within the crystal and after certain time delays, X-ray pulses (blue bars) probe reaction. XFELs has the initiated a newpart era of in the TRX This method results reducedLinear scattered intensities as only a portion of the X-ray pulse is used. As the crystals are damaged, XFEL experiments demand a serial way to introduce fresh samples into the X-ray interaction region This has led to the development of serial femtosecond crystallography. Lighter elements such as carbon, nitrogen, and oxygen, which are the main components of most proteins are less susceptible to radiation damage
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