1. Refined structures of the active Ser83→Cys and impaired Ser46→Asp histidine- containing phosphocarrier proteins 
Der-Ing Liao, Osnat Herzberg 
Structure 
Volume 2, Issue 12, Pages (December 1994)
DOI: /S (94)

2. Figure 1
The PTS pathway.
Structure 1994 2, DOI: ( /S (94) )

3. Figure 2
Folding topology of α/β jelly rolls: HPr, the RNA-binding domain of the U1 small nuclear ribonucleoprotein A (snRNP), andthe L7/L12 ribosomal protein (β–strands are indicated by arrows, helices by rectangles). Secondary-structure units are patterned to highlight pairwise interactions. For each of the examples, the scheme shows a global hairpin loop followed by a two-dimensional spiral description of the jelly roll topology, and finally a rolled-up three-dimensional version forming a right-handed jelly roll. This is not intended to imply an actual model for folding.
Structure 1994 2, DOI: ( /S (94) )

4. Figure 3
Stereoview of the differences around Asp30 between the two molecules in the asymmetric unit of the Ser46→Asp HPr crystal. Difference Fourier electron-density maps in the region of residues 29–31 of (a) molecule A and (b) molecule B. The coefficients 2Fo–Fc are used, and the phases are those calculated omitting Asp30 from the model. Both maps are contoured at a 1σ level. The environment of Asp30 in (c) molecule A and (d) molecule B shown in the same orientation. In both molecules, Asp69 interacts with Asp30, but because of the different main-chain conformation of Asp30, the modes of interaction are different. In addition, Lys28 of a symmetry-related molecule interacts with Asp69 in molecule A, but not in molecule B. The key electrostatic interactions are shown in thin solid lines.
Structure 1994 2, DOI: ( /S (94) )

5. Figure 3
Stereoview of the differences around Asp30 between the two molecules in the asymmetric unit of the Ser46→Asp HPr crystal. Difference Fourier electron-density maps in the region of residues 29–31 of (a) molecule A and (b) molecule B. The coefficients 2Fo–Fc are used, and the phases are those calculated omitting Asp30 from the model. Both maps are contoured at a 1σ level. The environment of Asp30 in (c) molecule A and (d) molecule B shown in the same orientation. In both molecules, Asp69 interacts with Asp30, but because of the different main-chain conformation of Asp30, the modes of interaction are different. In addition, Lys28 of a symmetry-related molecule interacts with Asp69 in molecule A, but not in molecule B. The key electrostatic interactions are shown in thin solid lines.
Structure 1994 2, DOI: ( /S (94) )

6. Figure 3
Stereoview of the differences around Asp30 between the two molecules in the asymmetric unit of the Ser46→Asp HPr crystal. Difference Fourier electron-density maps in the region of residues 29–31 of (a) molecule A and (b) molecule B. The coefficients 2Fo–Fc are used, and the phases are those calculated omitting Asp30 from the model. Both maps are contoured at a 1σ level. The environment of Asp30 in (c) molecule A and (d) molecule B shown in the same orientation. In both molecules, Asp69 interacts with Asp30, but because of the different main-chain conformation of Asp30, the modes of interaction are different. In addition, Lys28 of a symmetry-related molecule interacts with Asp69 in molecule A, but not in molecule B. The key electrostatic interactions are shown in thin solid lines.
Structure 1994 2, DOI: ( /S (94) )

7. Figure 3
Stereoview of the differences around Asp30 between the two molecules in the asymmetric unit of the Ser46→Asp HPr crystal. Difference Fourier electron-density maps in the region of residues 29–31 of (a) molecule A and (b) molecule B. The coefficients 2Fo–Fc are used, and the phases are those calculated omitting Asp30 from the model. Both maps are contoured at a 1σ level. The environment of Asp30 in (c) molecule A and (d) molecule B shown in the same orientation. In both molecules, Asp69 interacts with Asp30, but because of the different main-chain conformation of Asp30, the modes of interaction are different. In addition, Lys28 of a symmetry-related molecule interacts with Asp69 in molecule A, but not in molecule B. The key electrostatic interactions are shown in thin solid lines.
Structure 1994 2, DOI: ( /S (94) )

8. Figure 4
Superposition showing similarities between the Ser83→Cys HPr structure and the two monomers, A and B, of the Ser46→Asp HPr structure. Virtual bonds between Cα–atoms of Ser83→Cys HPr are shown in yellow and those of molecules A and B of Ser46→Asp HPr in red and blue respectively.
Structure 1994 2, DOI: ( /S (94) )

9. Figure 5
The active center of HPr. Superposition of the Ser83→Cys HPr (yellow) on molecule A (red) and molecule B (blue) of Ser46→Asp HPr.
Structure 1994 2, DOI: ( /S (94) )

10. Figure 6
Stereo representation of the difference Fourier electron density map associated with residues 15–17 in molecule B of Ser46→Asp HPr. The coefficients 2Fo–Fc are used, and the phases are those calculated omitting residues 15–17 from the model. The final model is displayed together with the map. The map is contoured at a 1σ level.
Structure 1994 2, DOI: ( /S (94) )

11. Figure 7
Stereoview of the superposition of the HPr active center inthe ion-free state, as seen in the Ser46→Asp mutant of HPr from B. subtilis (molecule B, filled bonds) and in HPr from S. faecalis (open bonds).
Structure 1994 2, DOI: ( /S (94) )

12. Figure 8
Stereo representation of the 2Fo–Fc difference Fourier electron-densitymap in the region of the Asp46 residues in the two molecules, A and B, of Ser46→Asp HPr, displayed with the final model. The map is contoured at a 1σ level.
Structure 1994 2, DOI: ( /S (94) )

13. Figure 9
Flow chart describing the steps of the molecular replacement. ψ, φ, κ, are the spherical polar angles; θ1 ,θ2, θ3, are the Eulerian angles as defined by Rossmann and Blow [52]. The two correlation values for the cross-rotation function correspond to the results before and after Patterson correlation refinement. The rotation angles of the highest 150 peaks of the cross-rotation function were refined.
Structure 1994 2, DOI: ( /S (94) )