X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
This study explores the possibility of measuring the dynamics of proteins in solution using X-ray photon correlation spectroscopy (XPCS) at nearly diffraction-limited storage rings (DLSRs). We calculate the signal-to-noise ratio (SNR) of XPCS experiments from a concentrated lysozyme solution at the...
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International Union of Crystallography
2019-09-01
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doaj-a3de92ce720447ddbc45655b27db0cd92020-11-25T00:41:04ZengInternational Union of CrystallographyIUCrJ2052-25252019-09-016579480310.1107/S2052252519008273tj5024X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage ringsJohannes Möller0Michael Sprung1Anders Madsen2Christian Gutt3European X-ray Free Electron Laser Facility, Holzkoppel 4, D-22869 Schenefeld GermanyDeutsches Elektronen Synchrotron DESY, D-22607 Hamburg, GermanyEuropean X-ray Free Electron Laser Facility, Holzkoppel 4, D-22869 Schenefeld GermanyDepartment Physik, Universität Siegen, D-57072 Siegen, GermanyThis study explores the possibility of measuring the dynamics of proteins in solution using X-ray photon correlation spectroscopy (XPCS) at nearly diffraction-limited storage rings (DLSRs). We calculate the signal-to-noise ratio (SNR) of XPCS experiments from a concentrated lysozyme solution at the length scale of the hydrodynamic radius of the protein molecule. We take into account limitations given by the critical X-ray dose and find expressions for the SNR as a function of beam size, sample-to-detector distance and photon energy. Specifically, we show that the combined increase in coherent flux and coherence lengths at the DLSR PETRA IV yields an increase in SNR of more than one order of magnitude. The resulting SNR values indicate that XPCS experiments of biological macromolecules on nanometre length scales will become feasible with the advent of a new generation of synchrotron sources. Our findings provide valuable input for the design and construction of future XPCS beamlines at DLSRs.http://scripts.iucr.org/cgi-bin/paper?S2052252519008273materials sciencestructural biologynanoscienceradiation damageSAXSstorage ringsX-ray photon correlation spectroscopysignal-to-noise ratio |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Johannes Möller Michael Sprung Anders Madsen Christian Gutt |
spellingShingle |
Johannes Möller Michael Sprung Anders Madsen Christian Gutt X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings IUCrJ materials science structural biology nanoscience radiation damage SAXS storage rings X-ray photon correlation spectroscopy signal-to-noise ratio |
author_facet |
Johannes Möller Michael Sprung Anders Madsen Christian Gutt |
author_sort |
Johannes Möller |
title |
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
title_short |
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
title_full |
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
title_fullStr |
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
title_full_unstemmed |
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
title_sort |
x-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings |
publisher |
International Union of Crystallography |
series |
IUCrJ |
issn |
2052-2525 |
publishDate |
2019-09-01 |
description |
This study explores the possibility of measuring the dynamics of proteins in solution using X-ray photon correlation spectroscopy (XPCS) at nearly diffraction-limited storage rings (DLSRs). We calculate the signal-to-noise ratio (SNR) of XPCS experiments from a concentrated lysozyme solution at the length scale of the hydrodynamic radius of the protein molecule. We take into account limitations given by the critical X-ray dose and find expressions for the SNR as a function of beam size, sample-to-detector distance and photon energy. Specifically, we show that the combined increase in coherent flux and coherence lengths at the DLSR PETRA IV yields an increase in SNR of more than one order of magnitude. The resulting SNR values indicate that XPCS experiments of biological macromolecules on nanometre length scales will become feasible with the advent of a new generation of synchrotron sources. Our findings provide valuable input for the design and construction of future XPCS beamlines at DLSRs. |
topic |
materials science structural biology nanoscience radiation damage SAXS storage rings X-ray photon correlation spectroscopy signal-to-noise ratio |
url |
http://scripts.iucr.org/cgi-bin/paper?S2052252519008273 |
work_keys_str_mv |
AT johannesmoller xrayphotoncorrelationspectroscopyofproteindynamicsatnearlydiffractionlimitedstoragerings AT michaelsprung xrayphotoncorrelationspectroscopyofproteindynamicsatnearlydiffractionlimitedstoragerings AT andersmadsen xrayphotoncorrelationspectroscopyofproteindynamicsatnearlydiffractionlimitedstoragerings AT christiangutt xrayphotoncorrelationspectroscopyofproteindynamicsatnearlydiffractionlimitedstoragerings |
_version_ |
1725287388156002304 |