Abstract

Serial crystallography (SX) is an emerging technique to determine macromolecules at room temperature. SX with a pump–probe experiment provides the time-resolved dynamics of target molecules. SX has developed rapidly over the past decade as a technique that not only provides room-temperature structures with biomolecules, but also has the ability to time-resolve their molecular dynamics. The serial femtosecond crystallography (SFX) technique using an X-ray free electron laser (XFEL) has now been extended to serial synchrotron crystallography (SSX) using synchrotron X-rays. The development of a variety of sample delivery techniques and data processing programs is currently accelerating SX research, thereby increasing the research scope. In this editorial, I briefly review some of the experimental techniques that have contributed to advances in the field of SX research and recent major research achievements. This Special Issue will contribute to the field of SX research.

Highlights

  • Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations

  • Radiation damage can be reduced through general application of data collection at cryogenic temperatures [5,6,7], but it does not completely annul radiation damage, and cryogenic structural information may be limited in terms of molecular dynamics [8]

  • In SX, radiation damage can be minimized because intense X-ray free electron laser (XFEL) or synchrotron X-rays are used to collect data by exposing the crystals to X-rays for a very short time and only once [4,12,13,14,15]

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Summary

Introduction

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. Traditional X-ray crystallography using single crystals has contributed to scientific developments, in the field of biological research, and in the medical industry, and has shown rapid growth over the past few decades [1,2]. Long-term exposure of X-rays to single crystals during data collection causes radiation damage by K-shell photoionization and Auger decay, which significantly reduces the quality of diffraction data and permits irreversible structural changes [3,4].

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