Figure 1.
Fig. 1. Stereodiagram of the 14-3-3 monomer
structure showing electron density for the pS-Raf-259 and R18
peptides. Helices forming the amphipathic groove are in white.
In red is an F[o] F[c] map
contoured at 2 calculated
for crystals soaked in the a) pS-Raf-259 or b) R18 peptide. The
maps are at 3.6 (A) and 3.35 Å (B) resolution using phases
calculated from the protein model before inclusion of peptide
atoms and improved by 4-fold noncrystallographic symmetry
averaging, histogram matching, and solvent flattening in DM
(25). The figure was produced with Bobscript (30) and Raster3D
(31).
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
16305-16310)
copyright 1998.
monomer
structure showing electron density for the pS-Raf-259 and R18
peptides. Helices forming the amphipathic groove are in white.
In red is an F[o] 
F[c] map
contoured at 2 
calculated
for crystals soaked in the a) pS-Raf-259 or b) R18 peptide. The
maps are at 3.6 (A) and 3.35 Å (B) resolution using phases
calculated from the protein model before inclusion of peptide
atoms and improved by 4-fold noncrystallographic symmetry
averaging, histogram matching, and solvent flattening in DM
(25). The figure was produced with Bobscript (30) and Raster3D
(31).