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"These unusual enzymes have been implicated in diseases ranging from Alzheimer’s disease to malaria, type II diabetes, cancer, Parkinson’s disease, cholera and tuberculosis."

This October, the new user facilities at the Cornell High-Energy Synchrotron Source (CHESS) will open their doors to researchers. This opening follows a major upgrade project, known as CHESS-U, which establishes CHESS as one of the world’s leading X-ray sources.

Last month, Linda Sapochack, NSF Division Director for the Division of Materials Research (DMR), Clark Cooper, Senior Advisor for Science and Head of the Office of Multidisciplinary Activities in the NSF Directorate for Mathematical and Physical Sciences, and NSF Program Director Guebre X. Tessema visited CHESS to see the newly upgraded facility.

A single human cell contains thousands of proteins that perform a vast array of functions, from fighting off viruses to transcribing DNA. By understanding the structure of these proteins, researchers can interpret their functions and develop methods for turning them on and off.

"The CHESS Users’ Meeting attracted a record number of 225 registered participants to the Cornell campus to look back at major milestones of the project and to discuss X-ray science enabled by the ambitious upgrade."

"By understanding how an essential enzyme is inactivated in an organism-specific manner, the researchers hope to contribute to the development of new anti-pathogenetic therapies."

Serial crystallography is a method for obtaining structural information on an atomic level of a protein, without the need for large protein crystals. Instead, small diffraction datasets are collected on many small protein crystals, which are usually easier to obtain than large ones. Serial crystallography is an ideal method for collecting diffraction data of proteins at room temperature, where the onset of radiation damage from the X-ray beam is rapid.

There is growing interest in the biological research community to characterize and understand the impact of high pressures, i.e. 100s of MPa, on the physical properties and function of biological macromolecules, e.g. proteins, viruses, lipids etc.