Cornell Lab Discovers New Regulatory Mechanism of Protein, Sheds Light on Importance of Cornell’s High Energy Synchrotron Source

Proteins are strikingly complex macromolecules, which control every aspect of molecular function in all living organisms, making them an interesting research target. The Ando Lab studies the structure of proteins, specifically enzymes, in order to understand their function, using structural techniques like x-ray diffraction and small-angle x-ray scattering. These techniques allow for the visualization of atomic and molecular structure of proteins. Small-angle x-ray scattering is a technique used to study the structure of proteins in solution. SAXS maintains an advantage over other techniques because it allows for the understanding of the movement of proteins; however a caveat to SAXS is its lower resolution, creating the need for combinatorial approaches to studying proteins such as combining SAXS with chromatography.

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Cornell Synchrotron Begins Two-Month X-Ray Run, Receives Mechanical Upgrades

By CAMILLE WANG
From last Wednesday to Dec. 8, the Cornell High Energy Synchrotron Source (CHESS), also known affectionately as the “world’s coolest microscope” by CHESS Director Prof. Joel Brock, applied and engineering physics, will be holding a scheduled x-ray run for users around the nation. CHESS is a high-intensity x-ray source funded by the National Science Foundation that is operated and managed by the University, driving research in fields spanning from electron behavior in a superconductor to arsenic poisoning in shrimp. These brief, high-power runs occur only three to four times a year, and a limited amount of time is available to accommodate all the research groups that would like to use the synchrotron for their projects, according to Prof. Kyle Lancaster, chemistry. Once scientists receive beam time, they often stay overnight to get the most out of their allotted time.