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. Author manuscript; available in PMC: 2018 Dec 25.
Published in final edited form as: Nat Chem Biol. 2018 Jun 25;14(9):853–860. doi: 10.1038/s41589-018-0085-5

Figure 3. Crystal structures of F2-Tyr157 CDO.

Figure 3

2Fo – Fc electron density was contoured at 1.2 σrms, with potential H-bond interactions (broken lines) shown. a, The active site of the 100% uncrosslinked F2-Tyr157 CDO structure in the substrate-free form. b, The active site of the 100% uncrosslinked F2-Tyr157 CDO structure in the substrate-bound form. c, The active site of the mature F2-Tyr157 CDO structure in the substrate-bound form. d, Overlaid active site of the 100% uncrosslinked F2-Tyr157 CDO structure in the substrate-free (2.40 Å resolution, grey) and substrate-bound (2.10 Å resolution, green) forms. e, Superimposition of the substrate-bound mature F2-Tyr CDO (1.95 Å resolution, pink) and 100% uncrosslinked structures (green). The L-cysteine substrate is labeled as CYS. The omit Fo-Fc electron densities for the water ligands (WAT) and the L-cysteine are shown in Supplementary Figure 2.