Extended Data Fig. 1: Crystals, ligand electron density maps, and packing of MT1.
From: Structural basis of ligand recognition at the human MT1 melatonin receptor
a, b, Bright field (a) and cross-polarized (b) images of representative MT1–2-PMT crystals, optimized for synchrotron data collection (representing three independent crystallization setups). c, Cross-polarized image of representative MT1–ramelteon crystals used for XFEL data collection (representing two independent crystallization setups). d, 2mFo − DFc ligand electron density maps of MT1 co-crystallized with 2-PMT (orange), 2-iodomelatonin (yellow), and agomelatine (cyan), contoured at 1.0σ (grey mesh). e, 2mFo − DFc (blue, contoured at 1.0σ) and mFo − DFc (green/red, ±3.5σ) electron density maps of MT1–ramelteon (ligand purple, protein yellow) illustrating the small, unassigned electron density close to N2556.52 that is tentatively attributed to the essential additive 2-propan-ol. The distance from this electron density to the closest ligand atom is approximately 4.8 Å. f, Packing of MT1–PGS crystallized in the P4 21 2 space group. The receptor is shown in green and the PGS fusion protein is shown in purple. g, Simulated annealing mFo − DFc omit maps (green mesh) of 2-PMT (orange sticks), 2-iodomelatonin (yellow), and agomelatine (cyan), contoured at 3.0σ.
