The kinetic dose limit in room-temperature time-resolved macromolecular crystallography.

Journal of Synchrotron Radiation
Marius SchmidtShailesh Tripathi

Abstract

Protein X-ray structures are determined with ionizing radiation that damages the protein at high X-ray doses. As a result, diffraction patterns deteriorate with the increased absorbed dose. Several strategies such as sample freezing or scavenging of X-ray-generated free radicals are currently employed to minimize this damage. However, little is known about how the absorbed X-ray dose affects time-resolved Laue data collected at physiological temperatures where the protein is fully functional in the crystal, and how the kinetic analysis of such data depends on the absorbed dose. Here, direct evidence for the impact of radiation damage on the function of a protein is presented using time-resolved macromolecular crystallography. The effect of radiation damage on the kinetic analysis of time-resolved X-ray data is also explored.

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Citations

Mar 3, 2012·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Matthew YoungblutA Andrew Pacheco
Dec 21, 2012·Journal of Synchrotron Radiation·Elspeth F Garman, Martin Weik
Jun 11, 2014·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Christopher KupitzPetra Fromme
Dec 7, 2013·Acta Crystallographica. Section D, Biological Crystallography·Marius SchmidtShailesh Tripathi
Jul 7, 2015·Acta Crystallographica. Section F, Structural Biology Communications·Ashtamurthy S PawateSarah L Perry
Jan 23, 2016·Structural Dynamics·Marius SchmidtJason Tenboer
Jul 3, 2013·The Journal of Physical Chemistry. B·Katherine M DavisYulia Pushkar
Mar 23, 2019·International Journal of Molecular Sciences·Marius Schmidt

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