 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 4]](aq5005fig4mag.jpg)
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Figure 4
Thermal stability of PA2949 in OG buffer measured by determination of enzymatic activity (a) and change in intrinsic fluorescence (b). The relative esterase activity and the derivative of esterase activity (ΔActivity/ΔT) as a function of temperature are shown in the upper and lower panels, respectively. 100% activity corresponds to the highest measured activity of PA2949. The fluorescence ratio (F350 nm/F330 nm) and the derivative of the fluorescence ratio [Δ(F350 nm/F330 nm)/ΔT] as a function of temperature are shown in the upper and lower diagrams, respectively. Dashed lines indicate calculated melting temperatures. Enzyme-activity results represent measurements of three independent experiments each with at least three samples. Standard deviations were within 10%. The fluorescence-based unfolding result is a representative single curve. |
![[Figure 4]](aq5005fig4.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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