Micromax 007hf cu

N42FTA (1 mM) was incubated for 1 h with PaFabA at 7 mg/ml before setting the plates. Crystals appeared at 20 °C after 2 days from a hanging drop of 2 μl of protein solution with 1 μl of reservoir solution containing 0.1 M lithium sulfate, 12% polyethylene glycol MME 5000, and 0.1 M sodium citrate (pH 5). Crystals were cryoprotected by supplementing the mother liquor with 15% glycerol.
Data were collected in-house using a Rigaku Micromax™-007HF Cu anode with VariMax optics and a Rigaku Saturn 944 + CCD detector. Data were processed with xia2 [46] , [47] , [48] (link), [49] , [50] (link). The structure was solved using the coordinates of the wild-type PaFabA [42] (link) and the programme Phaser [51] (link). PHENIX [52] (link) was used for autobuilding from molecular replacement solution. The model was adjusted with Coot [53] (link) after each round of refinement in REFMAC 5.6 from the CCP4 programme suite 6.2.0 with local NCS restraints (option in programme) and TLS parameters [54] (link) applied throughout. N42FTA was added to the model when the difference electron density was clear (Fig. 6a). Coordinates and topologies of ligand were generated by PRODRG [55] (link). The quality of the structure was checked with MolProbity [56] (link). Final refinement statistics are given in Table 1. Figures were drawn using PyMOL [57] .

X-ray data were collected in-house using an R-AXIS IV⁺⁺ image-plate system on a Rigaku MicroMax 007 HF Cu rotating-anode generator operating at 40 kV and 30 mA with Osmic VariMax HR optics. The crystal-to-detector distance was set to 100 mm and data were collected with oscillation steps of 1° (with an exposure time of 30 s) per image. The neutron crystal diffraction data were collected on the IMAGINE instrument, with a 20 h exposure time and images collected every 7°.