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Figure 5
Our FabH structure has alternative conformations for residues 249–258 at low occupancy. Our refined Ac-FabH + OCoA model is shown as white sticks with every other residue labeled, while the residues of FabH in PDB entry 1ebl chain A are shown in black. The Ac-FabH + OCoA σA-weighted 2mFo − DFc map is shown in blue and mFo − DFc maps are shown at +3σ in green and −3σ in red. Note how the residues for FabH in PDB entry 1ebl occupy the residual green positive density in our maps, suggesting that some fraction of the alternative conformation is populated in our crystals.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 79| Part 3| March 2023| Pages 61-69
https://doi.org/10.1107/S2053230X23001206
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