. 2020 May 22;8:21. doi: 10.1038/s41413-020-0095-2

Table 1.

Biochemical properties of PLS3 variants carrying OI-linked mutations

PLS3 construct	T_m /°C ± SE	K_d/μmol·L⁻¹ ± SD	[PLS3]_50%/μmol·L⁻¹ ± SD		pCa_50% ± SD
PLS3 construct	T_m /°C ± SE	K_d/μmol·L⁻¹ ± SD	EGTA	Ca²⁺	pCa_50% ± SD
Wild type	49.47 ± 0.72	7.41 ± 0.10	0.49 ± 0.28	2.97 ± 1.48	5.46 ± 0.14
L478P	44.93 ± 0.16	2.16 ± 0.36	n/a	n/a	n/a
N446S	46.87 ± 0.07	4.79 ± 0.56	0.58 ± 0.14	6.36 ± 2.46	6.44 ± 0.21
A253_L254insN	45.94 ± 0.95	3.77 ± 0.19	0.53 ± 0.16	2.09 ± 1.55	6.66 ± 0.17
A368D	43.38 ± 0.04	4.22 ± 0.81	0.47 ± 0.15	0.59 ± 0.09	n/a
E249_A250insI-L	41.93 ± 0.18	2.56 ± 0.46	0.10 ± 0.05	0.03 ± 0.04	n/a

T_m melting temperature determined by DSF, K_d equilibrium dissociation constant of PLS3 binding to F-actin, [PLS3]_50% bundling efficiency of PLS3 (concentration of PLS3 at 50% of F-actin bundled), pCa_50% Ca²⁺ sensitivity of PLS3 (-log[Ca²⁺] at 50% reduction in light scattering of actin bundles), SE standard error of the mean, SD standard deviation of the mean