Data Analytics at the Exascale for Free Electron Lasers
Linac Coherent Light Source (LCLS) is revealing biological structures in unprecedented atomic detail, allowing scientists to model proteins that play a key role in many biological functions. The results could help in designing new life-saving drugs while limiting side effects.
Biological function is profoundly influenced by dynamic changes in protein conformations and by interactions with molecules and other complexes – processes that span a broad range of timescales. Among many examples, these biological dynamics are central to the function of enzymes, cell membrane proteins and the macromolecular machines responsible for transcription, translation and splicing. Modern X-ray crystallography has transformed the field of structural biology by routinely resolving macromolecules at the atomic scale.
LCLS has already demonstrated a major advance in this area by resolving the structures of macromolecules that were previously inaccessible – using the new approaches of serial nanocrystallography and diffract-before-destroy with high-peak-power X-ray pulses. The high repetition rate of LCLS-II portends another major advance by revealing biological function through its unique capability to follow the dynamics of macromolecules and interacting complexes in real time and in native environments.
Advanced solution scattering and coherent imaging techniques will characterize, at the sub-nanometer scale, the conformational dynamics of heterogeneous ensembles of macromolecules – both spontaneous fluctuations of isolated complexes, and conformational changes that may be initiated by the presence of specific molecules, environmental changes, or by other stimuli.