Deciphering the intrinsic dynamics from the beam-induced atomic motions in oxide glasses

Chushkin, Yuriy

doi:10.1107/s1600577520009753

Cited by 9 publications

(10 citation statements)

References 26 publications

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“…S4 (b)). As such the effect is similar to the acceleration of the structural relaxation with dose rate observed in silica glass [25] and in other oxide glasses [26,38], and explained by breaking and reformation of atomic bonds [25][26][27] as a nonthermal effect [39].…”

supporting

confidence: 55%

“…3) as proposed in [27]. The observed linear relationship allows extrapolation to the limit of zero dose rate for our samples, which approaches the true intrinsic dynamics of the system [27]. To verify the validity of this approach we need to compare the estimated values with complementary measurements using other techniques.…”

mentioning

confidence: 80%

“…Based on the experimental fact that the beam-induced dynamics and the intrinsic dynamics are two independent and parallel relaxation processes [25,26] we determine the average relaxation rate 1/ τ r (at zero dose) versus dose rate (Insets in Fig. 3) as proposed in [27]. The observed linear relationship allows extrapolation to the limit of zero dose rate for our samples, which approaches the true intrinsic dynamics of the system [27].…”

mentioning

confidence: 94%

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Probing cage relaxation in concentrated protein solutions by XPCS

Chushkin¹,

Gulotta²,

Roosen-Runge³

et al. 2022

Preprint

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supporting

confidence: 55%

mentioning

confidence: 80%

mentioning

confidence: 94%

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Probing cage relaxation in concentrated protein solutions by XPCS

Chushkin¹,

Gulotta²,

Roosen-Runge³

et al. 2022

Preprint

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“…A beaminduced speeding up of dynamics has already been noted in oxide glasses (Ruta et al, 2017). In that case, a semi-empirical approach could be used to estimate the real À(q) in the zero X-ray dose limit (Chushkin, 2020).…”

Section: Figure 12mentioning

confidence: 89%

Performance of the time-resolved ultra-small-angle X-ray scattering beamline with the Extremely Brilliant Source

et al. 2022

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The new technical features and enhanced performance of the ID02 beamline with the Extremely Brilliant Source (EBS) at the ESRF are described. The beamline enables static and kinetic investigations of a broad range of systems from ångström to micrometre size scales and down to the sub-millisecond time range by combining different small-angle X-ray scattering techniques in a single instrument. In addition, a nearly coherent beam obtained in the high-resolution mode allows multispeckle X-ray photon correlation spectroscopy measurements down to the microsecond range over the ultra-small- and small-angle regions. While the scattering vector (of magnitude q) range covered is the same as before, 0.001 ≤ q ≤ 50 nm−1 for an X-ray wavelength of 1 Å, the EBS permits relaxation of the collimation conditions, thereby obtaining a higher flux throughput and lower background. In particular, a coherent photon flux in excess of 1012 photons s−1 can be routinely obtained, allowing dynamic studies of relatively dilute samples. The enhanced beam properties are complemented by advanced pixel-array detectors and high-throughput data reduction pipelines. All these developments together open new opportunities for structural, dynamic and kinetic investigations of out-of-equilibrium soft matter and biophysical systems.

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“…5b). Additional data with more dose rates could allow to develop new methods to estimate the di usion coe cients at zero dose rate [70]. Such an approach would allow for applying moderate doses and dose rates in MHz-XPCS experiments, which would increase the SNR and reduce the overall measurement time and sample consumption.…”

Section: Discussionmentioning

confidence: 99%

Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses

Reiser¹,

Girelli²,

Ragulskaya³

et al. 2022

Preprint

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X-ray free-electron lasers (XFELs) with megahertz repetition rate can provide novel insights into structural dynamics of biological macromolecule solutions. However, very high dose rates can lead to beam-induced dynamics and structural changes due to radiation damage. Here, we probe the dynamics of dense antibody protein (Ig-PEG) solutions using megahertz X-ray photon correlation spectroscopy (MHz-XPCS) at the European XFEL. By varying the total dose and dose rate, we identify a regime for measuring the motion of proteins in their rst coordination shell, quantify XFEL-induced e ects such as driven motion, and map out the extent of agglomeration dynamics. The results indicate that for dose rates below 1.16 kGy µs −1 in a time window up to 10 µs, it is possible to capture the protein dynamics before the onset of beam induced aggregation. We refer to this approach as correlation before aggregation and demonstrate that MHz-XPCS bridges an important spatio-temporal gap in measurement techniques for biological samples.

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Deciphering the intrinsic dynamics from the beam-induced atomic motions in oxide glasses

Cited by 9 publications

References 26 publications

Probing cage relaxation in concentrated protein solutions by XPCS

Probing cage relaxation in concentrated protein solutions by XPCS

Performance of the time-resolved ultra-small-angle X-ray scattering beamline with the Extremely Brilliant Source

Resolving molecular diffusion and aggregation of antibody proteins with megahertz X-ray free-electron laser pulses

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