Far-UV circular dichroism datasets describing salt dependent secondary structure of Clostridioides difficile endolysin catalytic domains

Description

This dataset contains far-UV circular dichroism data for the enzymatically active domains of two Clostridioides difficile–targeting bacteriophage endolysins, CD27L_EAD and PHICD111_20024_EAD. Measurements were performed at 25 °C using 10 µM protein in 20 mM Tris-HCl buffer (pH 7.0) containing 0, 50, 100, 150, or 200 mM NaF in a 0.5 mm path length cuvette. For each protein and NaF condition, three consecutive scans of the same sample were acquired. The dataset includes instrument-exported raw circular dichroism spectra (.csv), averaged spectra (.csv), high-tension signal traces (.csv), buffer blank spectra (.csv), processed mean residue ellipticity datasets (.xlsx), CDPro/CDSSTR output files (.out), and a summary table of α-helical content (.xlsx). CDPro analysis was performed using the CDSSTR algorithm with the SP43 reference set over 195–240 nm.

Steps to reproduce

1. Prepare CD27L_EAD and PHICD111_20024_EAD at 10 µM in 20 mM Tris-HCl (pH 7.0) containing 0, 50, 100, 150, or 200 mM NaF. 2. Record far-UV circular dichroism spectra from 195 to 260 nm at 25 °C using a 0.5 mm path length cuvette, collecting three consecutive scans of the same sample for each condition. 3. Record the corresponding buffer blank spectra and inspect the high-tension signal. 4. Subtract buffer spectra, convert the data to mean residue ellipticity, and analyze the 195–240 nm region using CDPro with the CDSSTR algorithm and the SP43 reference set. 5. Summarize the resulting α-helical content values from the three scans in the accompanying Excel table.

Institutions

• Ajou University

  Gyeonggi-do, Suwon

Categories

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