Journal article

A Perspective on Molecular Structure and Bond-Breaking in Radiation Damage in Serial Femtosecond Crystallography

Carl Caleman, Francisco Jares Junior, Oscar Granas, Andrew Martin

Crystals | MDPI | Published : 2020


X-ray free-electron lasers (XFELs) have a unique capability for time-resolved studies of protein dynamics and conformational changes on femto- and pico-second time scales. The extreme intensity of X-ray pulses can potentially cause significant modifications to the sample structure during exposure. Successful time-resolved XFEL crystallography depends on the unambiguous interpretation of the protein dynamics of interest from the effects of radiation damage. Proteins containing relatively heavy elements, such as sulfur or metals, have a higher risk for radiation damage. In metaloenzymes, for example, the dynamics of interest usually occur at the metal centers, which are also hotspots for damag..

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University of Melbourne Researchers


Awarded by Swedish Research Council

Awarded by Australian Research Council

Funding Acknowledgements

The Swedish Research Council (2018-00740), the Swedish Foundation for International Cooperation in Research and Higher Education (STINT), the Helmholtz Association through the Center for Free-Electron Laser Science at DESY, and the Australian Research Council's Centre of Excellence Programme. A.V.M. and C.C. acknowledges the funding support from the Australian Research Council Discovery Project grant (DP190103027).