Dimerization analysis of wild-type and mutant END domains by SEC/SLS and NMR.

ND—Not determined. Protein sample not stable and/or not suitable for NMR analysis. A Molecular weights were calculated from refractive index (RI) and right angle light scattering (RALS) data (Fig D in S1 Text). B For NMR, proteins without a Z-tag were analyzed. C 2D 1H,15N-HSQC spectrum indicates the presence of two populations, interpreted as an equilibrium between a folded dimer and the unfolded monomer of the END domain (Fig D in S1 Text). Dimerization analysis of wild-type and mutant END domains by SEC/SLS and NMR.