Abstract
X-ray-induced radiation damage is a limiting factor for the macromolecular crystallographer and data must often be merged from many crystals to yield complete data sets for the structure solution of challenging samples. Increasing the X-ray energy beyond the typical 10-15 keV range promises to provide an extension of crystal lifetime via an increase in diffraction efficiency. To date, however, hardware limitations have negated any possible gains. Through the first use of a cadmium telluride EIGER2 detector and a beamline optimized for high-energy data collection, it is shown that at higher energies fewer crystals will be required to obtain complete data, as the diffracted intensity per unit dose increases by a factor of more than two between 12.4 and 25 keV. Additionally, these higher energy data can provide more information, as shown by a systematic increase in the high-resolution cutoff of the data collected. Taken together, these gains point to a high-energy future for synchrotron-based macromolecular crystallography.
Highlights
Synchrotron-based macromolecular crystallography (MX) is the method of choice for determining the atomic structures of proteins and viruses, providing almost 90% of Protein Data Bank depositions over the last five years (Goodsell et al, 2020)
While these brighter beams enable structure solution from ever-smaller and more challenging crystals, it is at the expense of the one-crystal onestructure approach, as X-ray-induced damage precludes the collection of a complete data set from a single crystal (Smith et al, 2012)
In order to quantify the energy dependence of the diffraction efficiency of protein crystals, 29 low-dose data series were collected from 11 thermolysin crystals
Summary
Synchrotron-based macromolecular crystallography (MX) is the method of choice for determining the atomic structures of proteins and viruses, providing almost 90% of Protein Data Bank depositions over the last five years (Goodsell et al, 2020). The continual development of synchrotron beamlines and sources has resulted in the realization of smaller beam sizes and increased flux densities at the sample position (Owen et al, 2016) While these brighter beams enable structure solution from ever-smaller and more challenging crystals, it is at the expense of the one-crystal onestructure approach, as X-ray-induced damage precludes the collection of a complete data set from a single crystal (Smith et al, 2012). We further observe an increase in the resolution of data obtained for a given absorbed dose at higher energies
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