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Journal Article | PUBDB-2023-01521 |
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2023
MDPI
Basel
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Please use a persistent id in citations: doi:10.3390/cryst13081225 doi:10.3204/PUBDB-2023-01521
Abstract: Serial crystallography is a rapidly developing field that makes it possible to determine the structure of biomolecules at room temperature with atomic resolution. Numerous advances in detectors, data analysis pipelines, sample delivery methods, and crystallization protocols expand the scope of structural biology to understand the fundamental processes that take place in living cells. At the same time, all stages of experiments should be maximally optimized to avoid loss of beamtime. Thus, this paper proposes a strategy for optimizing beamtime utilization while using a fixed target sample delivery method such as chips. The strategy consists of two steps: first, a fast raster scan of the chip is performed to determine the positions of the crystals, and then small rotational series are measured at predetermined positions. Such an approach skips empty positions during data acquisition, saving valuable beam time and, as an additional consequence, reducing the volume of measured data.
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