Fig. 4 in Site-directed mutagenesis of β sesquiphellandrene synthase enhances enzyme promiscuity

Fig. 4. Structural analysis by circular dichroism (CD) of PmSTSΔ24WT and L454 mutants. Far-UV CD spectra (190–260 nm) of PmSTSΔ24 WT, PmSTSΔ24Y390S/L454G, PmSTSΔ24L454G and PmSTSΔ24L454A are shown. Buffer used was 20 mM Tris pH 8.0, 100 mM NaCl 2 mM βME. Protein concentration was 10 μM. Further secondary structure variations in percentages for each L454 mutant and WT were determined using the JASCO SSE program are presented in Table S2.