Figure 5.
Figure 5. Lattice interactions in the orthorhombic and cubic
crystal forms of the DAPK catalytic domain. a, Orthorhombic
form. Overview of the environment of the putative
peptide-binding region preceding the F-helix and the basic loop
linking 3
and helix C. Three symmetry mates colored blue, pink and cyan
make up the immediate surroundings of the loop region of each
DAPK molecule (red). Secondary structure elements are
represented as cylinders and arrows, and AMPPnP molecules and
four residues of the C-terminal streptavidin-tag visible in the
electron density maps are in a ball-and-stick representation. b,
Cubic form. The crystallographic asymmetric unit consists of
DAPK dimers related by a noncrystallographic two-fold rotation
axis running approximately along the vertical in the plane of
projection. Thus, basic loops and peptide binding regions of the
two molecules face each other.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2001,
8,
899-907)
copyright 2001.
3
and helix C. Three symmetry mates colored blue, pink and cyan
make up the immediate surroundings of the loop region of each
DAPK molecule (red). Secondary structure elements are
represented as cylinders and arrows, and AMPPnP molecules and
four residues of the C-terminal streptavidin-tag visible in the
electron density maps are in a ball-and-stick representation. b,
Cubic form. The crystallographic asymmetric unit consists of
DAPK dimers related by a noncrystallographic two-fold rotation
axis running approximately along the vertical in the plane of
projection. Thus, basic loops and peptide binding regions of the
two molecules face each other.