A new detector system for protein crystallography is now being developed based on an X-ray HARP-FEA (high-gain avalanche rushing amorphous photoconductor-field emitter array), which consists of an amorphous selenium membrane and a matrix field emitter array. The combination of the membrane avalanche effect with a single driven FEA has several advantages over currently available area detectors, including higher sensitivity, higher spatial resolution and a higher frame rate. Preliminary evaluation of the detector has been carried out and its effectiveness has been confirmed. Next, diffraction images were measured with continuous rotation of a protein crystal, and the images were compared with those measured by the existing CCD detector; the system successfully obtained high-spatial-resolution images. Using shutterless measurement, the total measurement time can be reduced significantly, making the method appropriate for high-throughput protein crystallography. The X-ray HARP-FEA detector is an attractive candidate for the next generation of X-ray area detectors.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2394816 | PMC |
http://dx.doi.org/10.1107/S0909049508006584 | DOI Listing |
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