Analysis of fold and dimerisation state of LEN and SMA.

(A) Far UV-CD spectra of VL confirms correctly folded recombinant protein, displaying native β-sheet structure with minimum around 220 nm. Units are presented as mean residue ellipticity. CD experiments were performed with 20 μM protein in 5 mM sodium phosphate (pH 7.5) at 4°C. (B) SEC-MALS chromatogram confirming the dimerisation state of LEN and SMA. Both VLs elute as single asymmetrical peaks at a volume of ~18.5 mL and ~19.5 mL on a HiLoad 16/60 Superdex 75 size exclusion column showing that a single species is present. Concentration of each protein was 1 mg/mL.