Anaerobic fixed-target serial crystallography

Rabe, P.; Beale, J.H.; Butryn, A.; Aller, P.; Dirr, A.; Lang, P.A.; Axford, D.N.; Carr, S.B.; Leissing, T.M.; McDonough, M.A.; Davy, B.; Ebrahim, A.; Orlans, J.; Storm, S.L.S.; Orville, A.M.; Schofield, C.J.; Owen, R.L.

doi:10.1107/S2052252520010374

Figure 4
Comparison of the anaerobic and O₂-exposed VioC structures. Close-up views of (a) a Polder omit map to 1.86 Å resolution of the active site of the VioC:Fe:2OG:Arg substrate complex structure reported in this study (PDB entry 6y0n) displayed at 2.0σ contour level, carved around the omitted arginine and 2OG, and (b) a Polder omit map of the active site of the VioC:Fe:2OG:(3S)-OH-Arg complex reported in this study (PDB entry 6y12) displayed at 3.0σ contour level, carved around the omitted (3S)-OH-Arg product and succinate highlighting the coordination of the substrate and product of VioC via D270, E170, Fe, S224, S156 and the conformationally flexible residue R334, which is solely present in the (3S)-OH-Arg product complex and disordered in the VioC:Fe:2OG:Arg substrate complex (Mitchell et al., 2017