2010 Volume 130 Issue 5 Pages 649-655
Nowadays, three-dimensional structure of protein becomes important to understanding and application of molecular mechanisms in enzyme reaction, signal transduction and other various biochemical processes. The amount of the information is now growing quantitatively and qualitatively, supported in part by the technical development of macromolecular crystallography. In the development, brilliant synchrotron radiation greatly contributes to enhance the accuracy and precision of diffraction data and the throughput of data collection. At SPring-8, JASRI and RIKEN collaborate to utilize the macromolecular crystallography beamlines and actualize these improvements. High throughput and routine analysis of protein structures is achieved by the development of automation system composed of sample exchange robotics and control software. The remote data collection system using the automation system and internet technology enhances efficiency and convenience of the beamlines. Moreover, the development of a rapid-readout complementary metal oxide semiconductor (CMOS) detector will improve throughput in data collection. On the other hand, data collection with high accuracy and precision is achieved by the utilization of brilliant X-ray produced from the in-vacuum undulator. Its brightest and stable beam enables high resolution data collection and 10 μm microbeam for microcrystals. Although the high brilliance severely damages protein samples, the users can estimate the degree of the damage and plan best data collection strategy.
