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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 σA-weighted 2FobsFcalc map was contoured at 1σ. (c) Stereo Cα trace of the internalin C structure. (b) was prepared using BOBSCRIPT (Esnouf, 1997BB7) and (c) and Fig. 4[link](b) were prepared using PyMOL (DeLano, 2002BB6).

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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