Ambient Crystallography - CHESS 2030 Workshop

"Not much biology happens at 100 Kelvin." This seemingly innocuous statement nonetheless has potentially hard-hitting consequences for modern structural biology. The advent of cryogenic crystallography in the 1980s revolutionized the study of biomacromolecular structure, as it ameliorated the ubiquitous problem of radiation damage of protein crystals. As proteins of interest became larger, more complex, and more sensitive to radiation damage, X-ray sources at storage ring light sources became brighter and more damaging, meaning collecting data at cryogenic temperatures became the de facto standard from the 1990s to today.

This workshop will seek to answer the question: what do we gain from collecting X-ray diffraction data at or close to physiological temperatures? The advent of protein crystallography at X-ray free electron lasers reinvigorated the study of protein crystallography at room temperature, enabling pump-probe dynamics experiments and the study of extremely small, poorly diffracting microcrystals. In order to deal with the effects of radiation damage, new techniques such as serial crystallography were developed.

Leaders in this field will be invited to discuss four broad topics: (1) the development of new methods for room temperature crystallography, including serial and single-crystal techniques; (2) applications of room temperature crystallography including time-dependent and dynamics experiments; (3) the differences between diffraction data collected at cryogenic temperature and room temperature; and (4) dealing with radiation damage associated with room temperature data collection.

Download the workshop flyer here.

All times are Eastern Daylight Time (GMT-4).