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Abstract

Serial crystallography has been driven mainly from sample requirements imposed by X-ray free electron lasers, however there is huge potential for new applications and experiments as well at regular (microfocus) synchrotron beamlines normally used for rotation based structure determination from single protein crystals. Our approach uses a combination of fixed target arrays for sample delivery of micron sized protein crystals and a fast, accurate translation system and thus allows high throughput serial data collection at high hit-rates and with low sample consumption. Data obtained in this approach yield high resolution structures and are collected at at room temperature with a low radiation dose per individual crystal, highly desirable for many proteins, where structures can normally suffer from radiation damage. Further the possibility to extend the approach to time-resolved crystallography for the study of protein dynamics on the millisecond timescale is shown.