Abstract
A recent paper in BMC Biology presents a general method for mix-and-inject serial crystallography, to facilitate the visualization of enzyme intermediates via time-resolved serial femtosecond crystallography (tr-SFX). They apply their method to resolve in near atomic detail the cleavage and inactivation of the antibiotic ceftriaxone by a β-lactamase enzyme from Mycobacterium tuberculosis. Their work demonstrates the general applicability of time-resolved crystallography, from which dynamic structures, at atomic resolution, can be obtained.See research article: https://bmcbiol.biomedcentral.com/articles/10.1186/s12915-018-0524-5.
Highlights
A recent paper in BMC Biology presents a general method for mix-and-inject serial crystallography, to facilitate the visualization of enzyme intermediates via time-resolved serial femtosecond crystallography
Serial femtosecond crystallography (SFX) methods that exploit slurries of microcrystals and the X-ray free electron lasers (XFELs) fs pulses are most often conducted at ambient temperature
SFX methods are well suited to couple structural biology with functional dynamics [2]
Summary
A recent paper in BMC Biology presents a general method for mix-and-inject serial crystallography, to facilitate the visualization of enzyme intermediates via time-resolved serial femtosecond crystallography (tr-SFX). And on the other hand, X-ray free electron lasers (XFELs) offer new opportunities because their unparalleled intensity makes it possible for even submicron size crystals to yield high quality structures. Serial femtosecond crystallography (SFX) methods that exploit slurries of microcrystals and the XFEL fs pulses are most often conducted at ambient temperature.
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