This project involves the construction of a beam line for macromolecular crystallography at the Center for Advanced Microstructures and Devices (CAMD) in Baton Rouge, Louisiana. A consortium of crystallographers from Texas, Oklahoma and Louisiana and physicists at CAMD/LSU will design, construct and maintain a state-of-the-art protein crystallography beam line for multiwavelength anomalous dispersion (MAD) and other diffraction experiments at CAMD.
Protein crystallography has provided invaluable insight into the molecular basis of life. These contributions range from a deep chemical understanding of enzyme mechanisms to the molecular basis of signal transduction and its role in cancer. An understanding of the molecular basis of biology will require structural information from many proteins. This is a daunting task because protein crystallography has traditionally been a challenging and labor-intensive methodology.
Synchrotron radiation has aided macromolecular crystallography in several ways. The superior intensity over laboratory sources has allowed the determination of structures of large proteins and viruses that could not be previously contemplated. The development of the synchrotron-based multi-wavelength anomalous dispersion (MAD) technique has streamlined the structure determination process. The number of structures solved by this methodology has grown exponentially in the last few years, placing great and ever increasing demand on the very few synchrotron beamlines. Regular and fast access to beam lines through lengthy application and waiting procedures now hinders the solution of new structures and other structural studies in a serious way.
The synchrotron at CAMD is in operation at an energy of 1.3-1.5 GeV. Together with an energy shifting wiggler which is being installed, the intensity of the beam for x-ray crystallography is estimated to be similar to that of a bending magnet at the National Synchrotron Light Source at Brookhaven National Laboratory. This should yield frame exposure times of under a minute for routine problems and up to 2 minutes for problem crystals. This is an order of magnitude faster than rotating anode times and has the extreme advantage of wavelength tunability for MAD experiments.
The beamline will serve as a regional research and training facility. Its close proximity to the consortium laboratories will expedite the solution of new structures and allow students new to crystallography to participate alongside senior students and postdocs in solution of protein or nucleic acid structures. A general user program will be established to allow access to non-consortium crystallographers.
