Taking advantage of new technology, the additional experimental stations at APS can accommodate many robotic and automated tools. This capability could enable researchers to conduct their studies from their home laboratories.
Smith credited the Protein Structure Initiative, a 10-year, $600 million program funded largely by NIGMS, for driving the development of automated systems that will enhance the performance of the new resources at the DOE facility.
The beamlines also are the first to utilize novel APS technology that splits a single X-ray beam into two and then manipulates each one so it's just as intense as the original.
"The ability to do two experiments simultaneously from the same light source is a big bonus," explained Smith. "It doubles the value of real estate at the synchrotron."
But where the new beamlines really show their power is in their ability to produce extremely fine X-ray beams. This feature enables researchers to capture data on molecules that have been challenging to work with in the past.
Already, the new facilities have produced exciting results. One research team has succeeded in generating a detailed structure of the bacteria-infecting HK97 virus--a notable achievement given that most viruses are complex and difficult to image at high resolutions. Knowing the structures of viruses and proteins and how they attach to other molecules will help researchers develop drugs that block those interactions.
"The properties of these X-ray beams are even better than we envisioned," said Charles Edmonds, Ph.D., NIGMS scientific director for the interagency project. "They will allow researchers to do new kinds of experiments, leading to even more ideas and questions to ask."
Structural biologists wi
Contact: Emily Carlson
NIH/National Institute of General Medical Sciences