Crystallography is a tool that allows structural biologists to discern protein structures to the highest degree of detail possible in three dimensions. The crystallography laboratory at UGA is probably the most advanced/enabling academic X-ray crystallography laboratory in the world in terms of both availability of state-of-the-art equipment and new technology development.
The group is led by Dr. Bi-Cheng Wang, a Georgia Research Alliance Eminent Scholar in Structural Biology. In 1997, Dr. Wang formed the Southeast Regional Collaborative Access Team (SER-CAT), a consortium for the access of synchrotron X-ray at the Advanced Photon Source (APS), Argonne National Laboratory outside Chicago. The aim of SER-CAT was to acquire laboratory space and to construct two very advanced X-ray beamline (stations) for the use of X-ray sources 10 million times more powerful than any X-ray sources in the home laboratory. One of the two stations has been operational since October 2002 after three years construction at a cost of approximately $7 million. As an extension of this initiative, but on a different front, Dr. Wang and his colleagues received an NIH award of $24 million for 5 years in October 2000 as a pilot Structural Genomics Center (SECSG) and an IBM SUR Award of $1 million in December 2001 for structural genomics related technology developments.
Dr. Wang, Director and PI of the NIH-funded Center, is now combining the SER-CAT capability, the IBM supercomputer, and structural genomics research in order to transform the traditionally research-oriented crystallography into a production-oriented high-throughput structural genomics analytical tool by an approach that he terms “Direct Crystallography.” Direct Crystallography means to determine the structure of proteins without the need of first labeling the sample. In a recent proof of concept experiment, a previously unknown structure was determined in just 4.5 hours from mounting the native (unlabeled) crystal on the X-ray detector and performing calculations on the IBM supercomputer to the output of the structural model.
In addition, Dr. Wang’s group is adopting nano-technologies and robotics aiming to miniaturize the crystallography processes. The goal is to be able to take proteins that can only be obtained in microgram quantity and consider them candidates in the near future for detailed structural analysis by X-ray crystallography.