 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](kw5080fig2mag.jpg)
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Figure 2
Backbone conformation in the active site of wild-type and E60Q FKBP12 and of the crystallographically non-equivalent monomers of FKBP12.6 in the P3121 crystal form. (a) shows the shift in backbone conformation and the reorientation of the Trp59 side chain that results from the altered hydrogen-bonding interactions of the side chain of residue 60 (Szep et al., 2009  ). A similar ∼90° rotation of the side-chain χ2 dihedral angle for Phe59 occurs between the two non-equivalent monomers in the P3121 crystal form of the cysteine-free variant of FKBP12.6, but without any corresponding alteration in the conformation of the backbone (b). |
![[Figure 2]](kw5080fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
