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. 2010 Feb 1;285(14):10616–10626. doi: 10.1074/jbc.M109.069070

TABLE 1.

Analytical ultracentrifugation of purified AIDA-I

Sedimentation velocity experiments were performed with purified wild-type or mutant AIDA-I diluted in 50 mm Tris-HCl, pH 8, containing 150 mm NaCl, 1 m NaCl, or 150 mm NaCl and 0.5% sodium deoxycholate. Sedimentation (c) and frictional (f/f0) coefficients and molecular mass were then determined by fitting the data from the sedimentation profiles, and the root mean square deviation (RMSD) from the best solution is indicated.

Protein Condition c(S) Molecular mass f/f0 RMSD
kDa
Wild-type Peak 1 with 150 mm NaCl 5.65 ± 0.234 133 ± 10 1.95a 0.00434
Peak 2 with 150 mm NaCl 7.27 ± 0.36 189 ± 12 1.95a 0.00434
1 m NaCl 4.375 ± 0.17 124 ± 8 1.77 0.00561
0.5% sodium deoxycholate 5.85 ± 0.2 135 ± 8 1.66 0.00542
I24 150 mm NaCl 5.13 ± 0.25 133 ± 10 1.89 0.00537

a This is an average frictional coefficient for the two species assumed to have similar shape; if the two species are constrained to be a monomer and a dimer of AIDA-I during the fitting, then two separate frictional coefficient can be calculated and are 1.69 for peak 1 and 2.08 for peak 2.