The proposed innovation is to develop a process that is sufficiently non-destructive to detect and analyze protein crystal defects and still permit a complete conventional diffraction analysis. By providing a quantitative means to evaluate protein crystals it will be possible to gain insights into how to improve their quality. By this process, experimental and theoretical research in utilizing the influence of microgravity in protein crystal growth can be advanced. The project is mainly concerned with the microscopic technique called X-ray topography. An understanding of the defect structures formed in macromolecular crystals is important if growth conditions are to be optimized. To a large extent the success of the semiconductor industry in growing large, defect free crystals of silicon and germanium is due to efforts similar to the effort we are proposing. While X-ray diffraction is an inherently destructive process for many protein crystals and in time will destroy a macromolecular crystal, the process that will be developed during this research is expected to be sufficiently non-destructive that after the topographic analysis it should be possible to perform a complete conventional diffraction analysis, determine the structure of the macromolecule, and evaluate the quality of the structural parameters which result.