Figure 1.
Figure 1 Crystal structure of bovine IF[1]-H49K. (A) Stereo view
of the 2.2 Å resolution 2F[o] - F[c] electron density map
calculated with CNS (contoured at 1.5 )
from residues 27 to 41 of the protein. (B) Stereo view of the
crystallographic packing. The four IF[1] monomers in the
asymmetric unit (A -D) are represented in red, sky blue, yellow
and dark blue, respectively. The origin of the unit cell and the
a, b and c axes are labelled 'o', 'a', 'b' and 'c',
respectively. (C) View along the crystallographic b-axis. (D)
Interactions between the two types of dimers. Dashed lines
represent the minimal inhibitory sequence of IF[1], which are
masked in the tetramers. C- and N-termini are indicated with the
letters C and N, respectively.
)
from residues 27 to 41 of the protein. (B) Stereo view of the
crystallographic packing. The four IF[1] monomers in the
asymmetric unit (A -D) are represented in red, sky blue, yellow
and dark blue, respectively. The origin of the unit cell and the
a, b and c axes are labelled 'o', 'a', 'b' and 'c',
respectively. (C) View along the crystallographic b-axis. (D)
Interactions between the two types of dimers. Dashed lines
represent the minimal inhibitory sequence of IF[1], which are
masked in the tetramers. C- and N-termini are indicated with the
letters C and N, respectively.