The most potent FabF inhibitor known to date, platensimycin, binds to the FabF thioester intermediate (Figure ). This intermediate state can be mimicked by mutating the active site Cys to either Gln or Ala. In both enzymes, PaFabF C164A and PaFabF C164Q, the binding site conformation is very similar (Figure and Table in supplementary information) and also binding affinities are comparable, suggestion that these enzyme variants are interchangeable. Here, we initially started working with PaFabF 164Q as the side chain of Gln more closely mimics the intermediate with the fatty acid bound. However, we later discovered that PaFabF C164A yields large, 3D crystals that diffract to a resolutions of up to 1.4 Å and can be used for more than 3 months, compared to PaFabF C164Q crystals that form as very thin plates which are difficult to handle and are only stable for 1 month. In addition, the resolution of the PaFabF C164A crystals is on average better. Thus, we switched to PaFabF C164A during the course of this study.