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Multiplexing methods in dynamic protein crystallography

MA. Klureza, Y. Pulnova, D. von Stetten, RL. Owen, GS. Beddard, AR. Pearson, BA. Yorke

. 2024 ; 709 (-) : 177-206. [pub] 20241024

Language English Country United States

Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.

Persistent link   https://www.medvik.cz/link/bmc25004185

Grant support
1764269 National Science Foundation

Time-resolved X-ray crystallography experiments were first performed in the 1980s, yet they remained a niche technique for decades. With the recent advent of X-ray free electron laser (XFEL) sources and serial crystallographic techniques, time-resolved crystallography has received renewed interest and has become more accessible to a wider user base. Despite this, time-resolved structures represent < 1 % of models deposited in the world-wide Protein Data Bank, indicating that the tools and techniques currently available require further development before such experiments can become truly routine. In this chapter, we demonstrate how applying data multiplexing to time-resolved crystallography can enhance the achievable time resolution at moderately intense monochromatic X-ray sources, ranging from synchrotrons to bench-top sources. We discuss the principles of multiplexing, where this technique may be advantageous, potential pitfalls, and experimental design considerations.

References provided by Crossref.org

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$a von Stetten, David $u European Molecular Biology, Laboratory (EMBL), Hamburg, Germany
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$a Owen, Robin L $u Diamond Light Source Ltd, Harwell Science and Innovation, Campus, Didcot, Oxfordshire, United Kingdom
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$a Beddard, Godfrey S $u School of Chemistry, University of Edinburgh, David Brewster Road, United Kingdom; School of Chemistry, University of Leeds, Woodhouse Lane, Leeds, United Kingdom
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