The use of synchrotron x-ray diffraction techniques to determine the atomic structures of protein crystals has become a well-established technique over the last decade for both scientific and industrial biological and pharmaceutical applications. Thousands of complex molecular structures have been deduced over the past decade, leading to a tremendous increase in pharmaceutical drug development, and an increase in the understanding of enzyme and other biological processes. The x-ray diffraction techniques to elucidate the molecular structures are used in combination with chemical analysis techniques that derive the chemical and biological function of the molecules. New demands are now being placed on the synchrotron macromolecular crystallography facilities by researchers and companies who propose to investigate hundreds of protein structures in a short time period with high-throughput data collection. For the study of large unit cell crystals, detectors with larger areas than are currently available are required. In addition, to study time-dependent phenomena, faster detectors are also required. The current-integrating signal-processing techniques now being used will need to be replaced with single photon-counting techniques, in order to achieve the higher sensitivities, larger dynamic range and faster data collection times that are being sought. We propose to develop an entirely new approach for detectors for macromolecular crystallography, by creating an integrated detector consisting of an Hgl2 thin film deposited directly onto CMOS imaging arrays. The Hgl2 film will act as a direct conversion medium for the diffracted x-rays. The charge carriers generated in the Hgl2 from the absorbed x-rays are sensed at the CMOS sensor as induced charge, then amplified and processed. ? ?
