Figure 1.
Fig. 1. Structure of CRY1-PHR and its disulfide bond. (A)
The structure of CRY1-PHR. Green, helices; purple, -strands;
dark blue, loop regions; orange, FAD cofactor; light blue,
AMP-PNP, which is not bound in the native structure. (B) The
disulfide bond in CRY1-PHR. The side chains of Cys-80 and
Cys-190 are shown, with the carbons in dark blue and the sulfurs
in yellow. Superimposed is a simulated-annealing omit map (F[o]
- F[c], contoured at 3 ) (28). Figs. 1 and 3
were generated by using PYMOL.
-strands;
dark blue, loop regions; orange, FAD cofactor; light blue,
AMP-PNP, which is not bound in the native structure. (B) The
disulfide bond in CRY1-PHR. The side chains of Cys-80 and
Cys-190 are shown, with the carbons in dark blue and the sulfurs
in yellow. Superimposed is a simulated-annealing omit map (F[o]
- F[c], contoured at 3 
) (28). Figs. 1 and 3
were generated by using PYMOL.