Abstract
X-ray television area detector diffractometry of single crystals has become an established technique for structure determination of biological macromolecules. As interest focuses on smaller crystals and larger unit cells, further improvements are needed in resolution and in signal-to-noise ratio; a detector diameter of about 150 mm has become desirable. These aims are being achieved by optimizing the X-ray phosphor, by a new design of image intensifier and by better optical coupling. New electronic circuitry is being developed to exploit the capability of these detectors of collecting complete diffraction data sets, containing about 0.5 Gb of information, in less than a minute at synchrotron radiation beam lines, some two to three orders of magnitude faster than by conventional methods with conventional X-ray sources.
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