Figure 1.
Fig. 1. (A) Final (2 F[o] F[c])
electron density at 1.85 Å resolution [1 level,
drawn with TURBO FRODO (37)], depicting the phosphate ion bound
at the Maf putative active site. Atoms of selected side chains
are colored yellow, blue, and red for carbon, nitrogen, and
oxygen, respectively, and oxygen atoms of water molecules are
shown as small red spheres. (B) Overall structure of the Maf
protein drawn with the program RIBBONS (38). The helices and
strands are
colored cyan and green, respectively, and are numbered. Loop
regions are colored orange, N and C termini are labeled, and a
yellow dot indicates the location of the disulfide bridge.
F[c])
electron density at 1.85 Å resolution [1 
level,
drawn with TURBO FRODO (37)], depicting the phosphate ion bound
at the Maf putative active site. Atoms of selected side chains
are colored yellow, blue, and red for carbon, nitrogen, and
oxygen, respectively, and oxygen atoms of water molecules are
shown as small red spheres. (B) Overall structure of the Maf
protein drawn with the program RIBBONS (38). The 
helices and
strands are
colored cyan and green, respectively, and are numbered. Loop
regions are colored orange, N and C termini are labeled, and a
yellow dot indicates the location of the disulfide bridge.