What is it about?

Our studies aim to explore the general role of fast motions in proteins that happen all the time. We expect that the principle is the same in all structured proteins and we hope that we will develop a model of proteins which can both predict and explain the nature of these motions.

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Why is it important?

The most important result of the study is that we can determine high-quality protein crystal structures at the FemtoMAX beamline. Their quality and resolution are similar to what can be seen at specialized macromolecular X-ray crystallography beamlines and intense X-ray free-electron lasers. The FemtoMAX beamline is gentle compared to X-ray free-electron lasers. We can be reasonably sure that protein is not damaged substantially by the X-ray beam, and we can record many images from the same sample. It is advantageous to look at a sample, do something with it, and look at it again. One can also repeat this process many, many times at the FemtoMAX beamline.


The repetition rate of the experiment is a key property of the beamline. We started at 2 Hz, we expect to continue with 10 Hz, but we already dream about 100Hz. The higher the repetition rate, the higher time and image resolution we can obtain.

Professor Gergely Katona
University of Gothenburg

Read the Original

This page is a summary of: High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection, Journal of Synchrotron Radiation, January 2021, International Union of Crystallography, DOI: 10.1107/s1600577520014599.
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