Wednesday, March 22, 2023, 1:30 pm — Videoconference / Virtual Event (see link below)
The advent of cryocrystallography made determining the high resolution of proteins using X-ray diffraction truly possible by reducing radiation damage of the samples. It is still the most widely used method, accounting for the vast majority of structures currently in the Protein Data Bank. But, with the advent of brighter X-ray sources (third and fourth generation synchrotrons and X-ray free electron lasers), the number of room temperature (RT), protein structures determined by X-ray diffraction is increasing once more. The development of technologies towards serial crystallography, including sample preparation, delivery, hardware and software advances, make these studies possible. RT structures show variations in conformations, highlighting structure-function relationships important for basic science and drug discovery. In this talk I will give an overview of some of the technologies and techniques we have worked on in recent years, including their application towards time-resolved experiments.
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