Mapping protein dynamics at high spatial resolution with temperature-jump X-ray crystallography.

ABSTRACT: Understanding and controlling protein motion at atomic resolution is a hallmark challenge for structural biologists and protein engineers because conformational dynamics are essential for complex functions such as enzyme catalysis and allosteric regulation. Time-resolved crystallography offers a window into protein motions, yet without a universal perturbation to initiate conformational changes the method has been limited in scope. Here we couple a solvent-based temperature jump with time-resolved crystallography to visualize structural motions in lysozyme, a dynamic enzyme. We observed widespread atomic vibrations on the nanosecond timescale, which evolve on the submillisecond timescale into localized structural fluctuations that are coupled to the active site. An orthogonal perturbation

SUBMITTER: Wolff AM 

PROVIDER: S-EPMC10624634 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature