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<p>We previously introduced the <i>spitrobot</i>, a protein crystal plunging system that enables reaction quenching via cryo-trapping with a time resolution in the millisecond range. Here we present the next generation, <i>spitrobot-2</i>, as an integrated benchtop device. User-friendliness has been improved by semi-automatic sample exchange. Moreover, a fully automated shutter shields the liquid nitrogen from the humidified environment, improving sample integrity. Most importantly, the cryo-trapping delay time has been reduced to 23 ms, making <i>spitrobot-2</i> twice as fast as the previous generation. This further expands the number of target systems that can be addressed by cryo-trapping time-resolved crystallography. Using 12 crystal structures of three independent model systems, we demonstrate successful cryo-trapping via observation of conformational changes and ligand binding within 25 ms. These improvements increase the convenient access to cryo-trapping, time-resolved X-ray crystallography empowering the MX community with efficient tools to advance research in structural biology.</p>

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Spitrobot-2 advances time-resolved cryo-trapping crystallography to under 25 ms

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年11月20日

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  • Maria Spiliopoulou,
  • Caitlin E. Hatton,
  • Martin Kollewe,
  • Jan-Philipp Leimkohl,
  • Hendrik Schikora,
  • Friedjof Tellkamp,
  • Pedram Mehrabi,
  • Eike C. Schulz

摘要

We previously introduced the spitrobot, a protein crystal plunging system that enables reaction quenching via cryo-trapping with a time resolution in the millisecond range. Here we present the next generation, spitrobot-2, as an integrated benchtop device. User-friendliness has been improved by semi-automatic sample exchange. Moreover, a fully automated shutter shields the liquid nitrogen from the humidified environment, improving sample integrity. Most importantly, the cryo-trapping delay time has been reduced to 23 ms, making spitrobot-2 twice as fast as the previous generation. This further expands the number of target systems that can be addressed by cryo-trapping time-resolved crystallography. Using 12 crystal structures of three independent model systems, we demonstrate successful cryo-trapping via observation of conformational changes and ligand binding within 25 ms. These improvements increase the convenient access to cryo-trapping, time-resolved X-ray crystallography empowering the MX community with efficient tools to advance research in structural biology.