What is it about?

In this paper, we investigate and quantify the experimental systematic errors for X-ray fluorescence spectroscopy of Cu amyloid-β peptide under in-situ electrochemical control. We introduce a new protocol to investigate radiation damage, thereby mitigating its impact while collecting data. The significance and impact of reducing and correcting systematic errors for X-ray fluorescence measurements in biological samples were clearly demonstrated in this paper.

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Why is it important?

Structural investigations of biological peptides using X-ray techniques are challenging due to the radiation sensitivity of the samples. It’s important to explore, quantify, and correct experimental errors to obtain highly accurate experimental measurements. This leads to more reliable structural investigations.

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This page is a summary of: Using XAS to monitor radiation damage in real time and post-analysis, and investigation of systematic errors of fluorescence XAS for Cu-bound amyloid-β, Journal of Applied Crystallography, February 2024, International Union of Crystallography,
DOI: 10.1107/s1600576723010890.
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