Skip to main content
. Author manuscript; available in PMC: 2025 Oct 3.
Published in final edited form as: Structure. 2024 Jul 30;32(10):1751–1759.e4. doi: 10.1016/j.str.2024.07.004

Fig. 5. Reduced protein stability of the CRX R90W mutant.

Fig. 5.

A. The R90W mutation modelled into the structure of the CRX-Ret4 complex. This mutation is breaking the bond between R90 and E55 and causes a steric clash between helices α1 and α3 potentially leading to protein instability. B. Steady-state Ret4 binding data for CRX R90W from three independent BLI assays (Mean±SD). The calculated KD for R90W/Ret4 interaction is 0.9±0.03 μM. Unpaired t test WT versus R90W, p***=0.0002. C. DLS thermal stability curves. Thermal stability of R90W CRX31–107 is significantly lower than the stability of WT CRX31–107.