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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Main Authors: Johannes Möller, Michael Sprung, Anders Madsen, Christian Gutt
Format: Article
Language:English
Published: International Union of Crystallography 2019-09-01
Series:IUCrJ
Subjects:
Online Access:http://scripts.iucr.org/cgi-bin/paper?S2052252519008273
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spelling 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
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