Schreiber, Frank
Preferred name
Schreiber, Frank
ORCID
Scopus Author ID
24722210600
3 results
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Publication Access status: Open Access , A pipeline for megahertz X-ray photon correlation spectroscopy on softmatter samples at the MID instrument of European XFEL(2026-02-22); ; ; ; In this article, we present the experimental protocol and data-processing framework for megahertz X-ray Photon Correlation Spectroscopy (MHz XPCS) experiments on soft matter samples implemented at the Materials Imaging and Dynamics (MID) instrument of the European X-ray Free-Electron Laser (EuXFEL). Due to the introduction of a standard configuration and the implementation of a highly automated data-processing pipeline, MHz-XPCS measurements can now be conducted and analyzed with minimal user intervention. A key challenge lies in managing the extremely large data volumes generated by the Adaptive Gain Integrating Pixel Detector (AGIPD) – often reaching several petabytes within a single experiment. We describe the technical implementation, discuss the hardware requirements related to effective parallel data processing and propose strategies to enhance data quality, in particular related to data reduction strategies and an improvement of the signal-to-noise ratio. Finally, we address strategies for making the processed data FAIR (Findable, Accessible, Interoperable, Reusable), in alignment with the goals of the DAPHNE4NFDI project.Source Type:Article23 9 - Some of the metrics are blocked by yourconsent settings
Publication Access status: Metadata only , Salt induced slowdown of kinetics and dynamics during thermal gelation of egg-yolk(2024); ; ; We investigated the effect of the NaCl concentration (0.3–2M) on the structure and dynamics of hen egg yolk at room temperature and during thermal gelation at temperatures in the range of 66–90 °C utilizing low-dose x-ray photon correlation spectroscopy in ultra-small angle x-ray scattering geometry. With an increase in the salt concentration, we observe progressive structural and dynamic changes at room temperature, indicating the disruption of yolk components such as yolk-granules and yolk-plasma proteins. Temperature- and salt-dependent structural and dynamic investigations suggest a delay in the gel formation and aggregation of yolk low-density lipoproteins with increasing ionic strength. However, the time–temperature superposition relationship observed in all samples suggests an identical mechanism underlying protein aggregation–gelation with a temperature-dependent reaction rate. The sol–gel transition time extracted from kinetic and dynamic information follows Arrhenius’s behavior, and the activation energy (460 kJ/mol) is found to be independent of the salt concentration.Source Type:Article3 - Some of the metrics are blocked by yourconsent settings
Publication Access status: Metadata only , X-ray driven and intrinsic dynamics in protein gels(2023); ; ; Source Type:Article1
