CCD-based synchrotron x-ray detector for protein crystallograph-performance projected from an experiment

The intense x radiation from a synchrotron source could, with a suitable detector, provide a complete set of diffraction images from a protein crystal before the crystal is damaged by radiation (2-3 min). An area detector consisting of a 40 mm dia. x-ray fluorescing phosphor, coupled with an image intensifier and lens to a CCD image sensor, was developed to determine the effectiveness of such a detector in protein crystallography. The detector was used in an experiment with a rotating anode x-ray generator. Diffraction patterns from a lysozyme crystal obtained with this detector are compared to those obtained with film. The two images appear to be virtually identical. The flux of 10/⁴ x-ray photons/s was observed on the detector at the rotating anode generator. At the 6-GeV synchrotron being designed at Argonne, the flux on an 80×80 mm² detector is expected to be ≫ 10⁹ photons/s. The projected design of such a synchrotron detector shows that a diffraction-peak count ≫ 10⁶ could be obtained in ˜0.5 s. With an additional ˜0.5 s readout time of a 512×512 pixel CCD, the data acquisition time per frame would be ˜1 s so that ninety 1^o diffraction images could be obtained, with approximately 1% precision, in less than 3 min.