1. A distinct 14 residue site triggers coiled ‐ coil formation in cortexillin I by Michel O. Steinmetz, Alexander Stock, Therese Schulthess, Ruth Landwehr, Ariel Lustig, Jan Faix, Günther Gerisch, Ueli Aebi, and Richard A. Kammerer EMBO J. Volume 17(7):1883-1891 April 1, 1998 ©1998 by European Molecular Biology Organization

2. Design and preparation of N ‐ and C ‐ terminal deletion constructs from Ir. (A) Amino acid sequence of Ir. Heptad repeats were assigned according to the COILS algorithm (Lupas et al., 1991) and are shown in blocks of seven amino acid residues denoted abcdefg. Michel O. Steinmetz et al. EMBO J. 1998;17:1883-1891 ©1998 by European Molecular Biology Organization

3. Electron microscopic analysis of recombinant cortexillin Ir homodimer rods. Michel O. Steinmetz et al. EMBO J. 1998;17:1883-1891 ©1998 by European Molecular Biology Organization

4. CD measurements of recombinant cortexillin Ir and various deletion constructs. Michel O. Steinmetz et al. EMBO J. 1998;17:1883-1891 ©1998 by European Molecular Biology Organization

5. Electron micrographs of glycerol ‐ sprayed/rotary metal ‐ shadowed recombinant (A) cI ‐ 310 and (B) cI ‐ 324 cortexillin I fragments which were designed so as to contain the N ‐ terminal globular head domain (residues 1–226) and 12 or 14 heptad repeats, respectively,... Michel O. Steinmetz et al. EMBO J. 1998;17:1883-1891 ©1998 by European Molecular Biology Organization

6. CD analysis of the 16 residue peptide cI ‐ t. Michel O. Steinmetz et al. EMBO J. 1998;17:1883-1891 ©1998 by European Molecular Biology Organization