This data article presents salt dependent far-UV circular dichroism datasets for the enzymatically active domains of two Clostridioides difficile –targeting bacteriophage endolysins, CD27LEAD and PHICD111₂0024EAD. The dataset comprises sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) images documenting protein sample purity, far-UV circular dichroism spectra recorded from 195 to 260 nm, and secondary structure content estimates obtained by CDPro analysis over 195–240 nm. Circular dichroism measurements were performed at 25°C using 10 µM protein in 20 mM Tris-HCl (pH 7. 0) containing 0, 50, 100, 150, and 200 mM NaF. For each protein and NaF condition, spectra were acquired as three consecutive scans of the same sample. Baseline-corrected spectra were converted to mean residue ellipticity. The resulting mean residue ellipticity data were averaged for visualization, and α-helical content was estimated by CDPro analysis of each scan over 195–240 nm. The repository provides instrument-exported CSV files containing wavelength-resolved circular dichroism signals in millidegrees together with acquisition information. Processed mean residue ellipticity datasets (Excel files), CDPro/CDSSTR output files (. out), and summary tables of α-helical content are also provided. SDS-PAGE images documenting sample purity are presented as figures in this article.
Hwang et al. (Fri,) studied this question.