Figure 3.
Figure 3 A stereoview illustrating the conformation of helix
3
(shown without side chains, except Lys136 and Arg138) in
LlPR-10.2A (molecule A). A kink of almost 60° in the middle
of the helix is well supported by the 2F[o] - F[c]
electron-density map (contoured at the 1.0 level).
The helix is stabilized by salt bridges formed by Lys136 and
Arg138 and by hydrophobic interactions with the -sheet
(not shown).
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
99-0)
copyright 2005.
3
(shown without side chains, except Lys136 and Arg138) in
LlPR-10.2A (molecule A). A kink of almost 60° in the middle
of the helix is well supported by the 2F[o] - F[c]
electron-density map (contoured at the 1.0 
level).
The helix is stabilized by salt bridges formed by Lys136 and
Arg138 and by hydrophobic interactions with the 
-sheet
(not shown).