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X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
by
Gutt, Christian
, Sprung, Michael
, Möller, Johannes
, Madsen, Anders
in
Detection equipment
/ Lysozyme
/ Macromolecules
/ materials science
/ nanoscience
/ Photon correlation spectroscopy
/ Photons
/ Proteins
/ radiation damage
/ Research Letters
/ SAXS
/ Signal to noise ratio
/ Spectroscopy
/ Spectrum analysis
/ storage rings
/ structural biology
/ X-ray photon correlation spectroscopy
2019
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X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
by
Gutt, Christian
, Sprung, Michael
, Möller, Johannes
, Madsen, Anders
in
Detection equipment
/ Lysozyme
/ Macromolecules
/ materials science
/ nanoscience
/ Photon correlation spectroscopy
/ Photons
/ Proteins
/ radiation damage
/ Research Letters
/ SAXS
/ Signal to noise ratio
/ Spectroscopy
/ Spectrum analysis
/ storage rings
/ structural biology
/ X-ray photon correlation spectroscopy
2019
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While trying to remove the title from your shelf something went wrong :( Kindly try again later!
Do you wish to request the book?
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
by
Gutt, Christian
, Sprung, Michael
, Möller, Johannes
, Madsen, Anders
in
Detection equipment
/ Lysozyme
/ Macromolecules
/ materials science
/ nanoscience
/ Photon correlation spectroscopy
/ Photons
/ Proteins
/ radiation damage
/ Research Letters
/ SAXS
/ Signal to noise ratio
/ Spectroscopy
/ Spectrum analysis
/ storage rings
/ structural biology
/ X-ray photon correlation spectroscopy
2019
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X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
Journal Article
X-ray photon correlation spectroscopy of protein dynamics at nearly diffraction-limited storage rings
2019
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Overview
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.
Publisher
International Union of Crystallography
Subject
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