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. Author manuscript; available in PMC: 2018 Dec 30.
Published in final edited form as: Cell Syst. 2017 Nov 1;5(5):518–526.e3. doi: 10.1016/j.cels.2017.10.004

Table 1: Parameters for the allosteric sigmoidal fit of adsorption of SpoVMWT and SpoVM variants onto differently curved surfaces as measured by flow cytometry.

Bmax, maximal binding value; h, Hill coefficient; K1/2, concentration of protein producing half-maximal binding; MESF, molecules of equivalent soluble fluorochrome. Errors are SEM (n=3 independent trials, each trial containing data from >30,000 SSLBs). “N/D” indicates “not determinable”.

Protein Bead diam. (μm) Bmax (MESF/μm2) h K1/2 (μM)
SpoVM-FITC 2 3,920 (± 100) 4.3 (± 0.8) 0.58 (± 0.03)
8 4,450 (± 200) 2.2 (± 0.3) 1.0 (± 0.07)
SpoVMP9A-FITC 2 3,040 (± 70) 1.5 (± 0.1) 0.58 (± 0.03)
8 3,340 (± 480) 1.1 (± 0.3) 0.84 (± 0.26)
SpoVML8P,P9A-FITC 2 3,640 (± 190) 1.9 (± 0.2) 1.67 (± 0.13)
8 5,140 (± 750) 2.4 (± 0.4) 3.40 (± 0.53)
SpoVMP9A,K10P-FITC 2 4,350 (± 310) 1.8 (± 0.2) 1.81 (± 0.20)
8 N/D 1.1 (± 0.3) N/D
SpoVMP9A,F11P-FITC 2 4,150 (± 160) 2.5 (± 0.3) 1.48 (± 0.07)
8 N/D 1.2 (± 0.2) N/D
SpoVMP9G-FITC 2 2,950 (± 80) 3.9 (± 0.9) 0.41 (± 0.03)
8 3,090 (± 560) 1.1 (± 0.4) 0.83 (± 0.33)