Figure 1.
Figure 1 (a) Schematic drawing of the domain structure of
internalin C. (b) Electron density around Phe146, one of only
two exposed hydrophobic residues on the receptor-binding surface
of internalin C; also shown are adjacent leucine residues that
contribute to the hydrophobic core of the LRR domain. The 2.0
Å resolution [A]-weighted
2F[obs] - F[calc] map was contoured at 1 .
(c) Stereo C^ trace
of the internalin C structure. (b) was prepared using BOBSCRIPT
(Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15,
132-134.]) and (c) and Fig. 4-(b) were prepared using PyMOL
(DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular
Visualization System. DeLano Scientific, San Carlos, CA, USA.
http://www.pymol.org .]).
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
1287-1293)
copyright 2006.
[A]-weighted
2F[obs] - F[calc] map was contoured at 1 
trace
of the internalin C structure. (b) was prepared using BOBSCRIPT
(Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15,
132-134.]) and (c) and Fig. 4-(b) were prepared using PyMOL
(DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular
Visualization System. DeLano Scientific, San Carlos, CA, USA.
http://www.pymol.org .]).