Fig. 1. 2D depiction of a tessellation structure. The thick line is the SA surface defined by rolling the solvent (small, black circles) along the VDW surface, the rectangle is the bounding box for the tessellation run, and the tessellation is the Delaunay triangulation of points placed between the two sets of atoms. There is a dashed circle around one of the vertices representing the vertex radius used to create the tessellation.

Fig. 2. Tessellation of myoglobin inaccessible cavities. Xenon binding sites are labeled.

Fig. 3. Tessellation of the tRNA^Asp–synthetase interface. (A) The catalytic domain of the synthetase is shown in blue, and the ACB domain is shown in green. The tRNA^Aspis colored by structural composition: acceptor stem (orange), D-arm (white), AC arm (red), and the variable region and T-arm (purple). The tessellation in gray shows the areas within the interface that are potentially accessible to H₂ O. The four interaction sites are labeled. (B) Secondary structure of tRNA^Asp colored by synthetase interaction site: site 1 (red), site 2 (blue), site 3 (orange), site 4 (green), and G30 (purple). Black is used for non-interacting bases.

Fig. 4. Amino acids within 5 Å of the tRNA are shown in surface representation and colored from high (blue) to low (red) conservation across the Eucarya. Nucleotides within 5 Å of the protein are shown in purple except for the anticodon bases, which are yellow.

Fig. 5. Tessellation of the ammonia pore of the hisH–hisF complex. (A) The hisH–hisF complex of S. cerevisiae. HisH is shown with red -helices and orange -strands, and hisF is shows with blue -helices and purple -strands. The pore shown was created using HOLE and depicted with spheres of uniform 2.0 Å radius (Smart et al., 1993). (B) Tessellation of the closed pore. (C) Tessellation of the open pore. (D) Tessellation of the open pore colored by difference from the closed pore tessellation. The most stable regions are colored blue, and the highest moving regions are red.