Far-UV CD analysis of <i>r</i>EPclA after purification by SEC.

<p>(<b>A</b>) CD spectra at 4°C, 45°C, 55°C and 4°C after immediately cooling back the sample (see text). The vertical axis measures mean residue ellipticity Θ in degrees cm² dmol^-1. The CD data was collected between 195 and 260 nm, with a protein concentration of 0.04 mg/ml (4°C) or 0.3 mg/ml (the rest) in 10 mM Tris, 150 mM NaCl, pH 7.4. Measurements were taken in a 0.5 mm path length cell. (<b>B</b>) Thermal denaturation of <i>r</i>EPclA monitored by CD at 216 nm (the maximum between the two minima at 208 and 224 nm). The CD was measured as a function of increasing temperature between 20°C and 75°C, with a protein concentration of 0.3 mg/ml in 10 mM Tris, 150 mM NaCl, pH 7.4, and a heating rate of 0.33°C/min.