Current research in structural biology is focused on understanding the role of enzymes and proteins in regulating cellular metabolism and the way drugs bind to proteins so that more effective drugs which can inhibit viral activity may be developed. Neutron crystallography provides a unique way of defining molecular geometry, essential knowledge if we are to fully understand the behavior of many pharmaceutical and biological molecules. Neutron crystallography holds great promise, as neutrons interact more strongly with nuclei than x-rays. While x-ray diffraction gives excellent structural information, neutron diffraction provides complimentary information regarding the positions of light atoms such as hydrogen. Modem neutron sources such as the Spallation Source being built at ORNL hold great promise for macromolecular crystallography by providing unprecedented levels of neutron fluxes. They have not yet realized their potential due to the lack of an appropriate position sensitive sensor, which limit the practical implementation and growth of diffraction experiments. To address these needs we propose to develop a novel position sensitive neutron detector, based on a new high-resolution, high-efficiency, large area, micro-columnar scintillator coupled to a CCD readout. The proposed detector will provide excellent gamma discrimination, detection efficiency, spatial resolution, and dynamic range superior to current systems.
The proposed detector would offer several performance advantages over the existing large area neutron sensors for structural biology and would be relatively inexpensive to manufacture. This new detector technology would find widespread use in nuclear physics research, material science, biomedical research, and non-destructive testing using neutron radiography and industrial tomography.
