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![[Figure 5]](qt5002fig5mag.jpg)
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Figure 5
A fluorescence-based thermal shift assay reveals experimental conditions that stabilize PknG. (a) Melting curves of PknG at different pH values (after `min–max normalization' in the Load Input step, a transformation that scales the values between 0 and 1 without changing the shape of the curve). (b) Melting temperatures (Tm) from the curves in (a) estimated using the two-state reversible unfolding model implemented in MoltenProt. (c) Melting curves (after `min–max normalization') of PknG under different experimental conditions, including the addition of ligands (AX2017 in 1% DMSO, ATPγS and Mg) or a 1:1 mixing of PknG with the crystallization condition (CC) used by Lisa and coworkers to obtain the crystal structure with PDB code 4y12. The complete list of experimental conditions can be found in Section 4.1.4 ![[link]](../../../../../../logos/arrows/d_arr.gif) . (d) Melting temperatures (Tm) from the curves in (c) estimated using the two-state reversible unfolding model implemented in MoltenProt. |
![[Figure 5]](qt5002fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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