News

As antibiotic resistance rises, the search for new antibiotic strategies has become imperative. In 2013, the Centers for Disease Control estimated that antibiotic resistant bacteria cause at least 2 million infections and 23,000 deaths a year in the U.S.; a recent report raised the likely mortality rate to 162,044.

In one of the first commissioning experiments since the upgrade of the facility, the team of Aaron Finke and collaborators measured the first crystal structure at CHESS beamline ID7B2.  The beamline provided excellent quality data and a good refined structure from a fluoroacetate dehalogenase crystal was obtained as shown below. Further commissioning is underway. Even at this early stage, ID7B2 is definitely geared up to be a world-class beamline.

First Light at CHESS into Sector 7B2 Hutch!

Proteins are molecular machines that participate in the vast majority of activities that occur in any living system.  To carry out their functions, they undergo dynamic changes in structure and shape and interact with other molecular systems.  Characterizing these intramolecular motions provides insight into the molecular basis of protein function and, in turn, can result in a deeper understanding of a vast range of physiological functions.

X-ray crystallography allows determination of the atomic structure of proteins, information that is essential to understanding the proteins. It was thought that there was a minimum size of crystal that could be used at storage ring x-ray sources. This paper shows that the minimum size barrier can be overcome.

A naturally occurring antibiotic called kanglemycin A is effective against Mycobacterium tuberculosis, the bacteria that cause tuberculosis, even in drug-resistant strains, according to an international team of researchers who used chemistry, molecular biology, microbiology, and X-ray crystallography to show how the compound maintains its activity.

Christopher Flynn, a fourth year student majoring in Physics and Mathematics at Fort Lewis College, and a SUnRiSE student at Cornell this summer, is contributing to the design of microfluidic mixing chips which could significantly enhance our understanding of proteins and living cells.

In an era when our most detailed pictures of biomolecules come from frozen or crystalline samples, biological small angle X-ray solution scattering (BioSAXS) is more essential than ever as a tool for learning how molecules actually behave under realistic biological conditions in the liquid state.