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Line five of Figure 9 legend contained an error in which two symbols were incorrectly labelled. The correct legend is shown below.

Figure 9. Activation and inactivation properties of a COOH-terminal truncated version of α_1E (α_1EΔ, amino acids 1–1871) that lacks a putative β binding site. All measurements for both α_1E and α_1EΔ are in 10 mM Ba²⁺. (A) Traces illustrating activation of ionic currents for α_1EΔα₂δ (cell 375_19) or α_1EΔβ_2aα₂δ (cell 370_6) using the same voltage protocol as in Fig. 2. Data are shown for test pulse potentials of −30, −20, −10, 10, and 50 mV. (B) Comparison of G-V for α_1EΔ and α_1E indicates that modulation of α_1EΔ activation by β subunits is preserved. Symbols correspond to data for α_1EΔ and wild-type α_1E (α_1EΔβ_2aα₂δ, ○, n = 4; α_1EΔα₂δ, •, n = 11; α_1Eα₂δ, □, n = 11; and α_1Eβ_2a, ▪, n = 8). Lines are single-Boltzmann fits to the α_1Eα₂ and α_1Eβ_2a data with fit parameters z = 2.4, V_1/2 = −10.1; and z = 3.4, V_1/2 = −18.2, respectively. The shift in V_1/2 values relative to Fig. 6 C corresponds to a surface potential shift between 10 mM (used here) and 2 mM Ba²⁺ (Fig. 6). (C) Steady state inactivation. Traces after a 20-s prepulse (as in Fig. 7) to the indicated potentials are shown for α_1EΔ in combination with α₂δ (cell 376_9), β₃ (cell 375_4), β_2aα₂δ (cell 370_11), and β₃α₂δ (cell 371_10). (D) Comparison of h(∞)-V relations for α_1EΔ (symbols) and α_1E (same data as in Fig. 7, shown as lines connecting mean data values, without explicit reproduction of data points as symbols). Symbols correspond to the following constructs: α_1EΔα₂δ, •; α_1EΔβ_2aα₂δ, ○; α_1EΔβ₃, ▿; α_1EΔβ₃α₂δ, ×. Data for α_1E is shifted by −7 mV to overlay the α_1EΔ data. Average fit values and cell numbers are summarized in Tables V (G-V) and III [h(∞)-V] for both α_1E and α_1EΔ.