Table 4 AUC-SV: summary of the isotherm sedimentation velocity analysis of Ozz–EloBC in 10 mM sodium phosphate, 1.8 mM potassium phosphate pH 7.2, 137 mM NaCl and 0.27 mM KCl buffer at 20 °C. Model: monomer–dimer self-association.

From: Biophysical and functional study of CRL5Ozz, a muscle specific ubiquitin ligase complex

Samplea

Conc (µM)a

KD12 (µM)b

RMSDc

Ozz–EloBC

13.3, 5.3, 1.8

0.70 [0.43, 1.07]

0.0930

  1. aTotal concentration of the integrated monomer–dimer c(s) peaks.
  2. bDissociation constant KD12 of the monomer–dimer self-association reaction. For the isotherm signal‐weighted-average sedimentation coefficient values were obtained by integration of the c(s) distributions between 3 and 7 S at various concentrations17,22.
  3. The s‐values for monomer and dimer, s1 and s2 (3.82 S and 5.75 S) were fixed while the K12 the equilibrium association constant was optimized in the fit (Theoretical molar mass: 57,285 Da). Errors of the constant represent the 68% confidence interval (CI) using an automated surface projection method23.
  4. cRoot mean square deviation of the fit, units in fringes for the reversible dimer formation.
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