Fig. 2: High-resolution crystal structures of JIP1-SH3 variants.
From: Visualizing protein breathing motions associated with aromatic ring flipping
a–d, Crystal structures showing the conformation of Y526, the corresponding unbiased electron density maps (Fo–Fc) of Y526 and its surrounding residues, and the Newman projection along the Cβ–Cγ bond of Y526 in the V517L (a), A541L (b), H493A (c) and V517A (d) variants of JIP1-SH3. Dashed lines indicate CH–π (black) and π–π (red) interactions. Residue numbers in red indicate the site of mutation. The wild-type JIP1-SH3 structure is shown as a reference in the centre.
