Crystal Structure of Dicamba Monooxygenase with Non-heme Iron and Dicamba

Dicamba monooxygenase: structural insights into a dynamic Rieske oxygenase that catalyzes an exocyclic monooxygenation.

Rosenbaum-Rock monochromator with high-resolution double-crystal Si(220) sagittal focusing.

The purified protein was concentrated to 10-20 mg/ml and buffer exchanged into 25 mM Tris-HCl, pH 8.0, 30-50 mM NaCl, 25 mM sodium citrate. DMO crystals were grown using the vapor diffusion by sitting drop method, with a reservoir solution of 8-11% PEG 6000, 100 mM sodium acetate buffer-pH 5.5, 1 M LiCl, and 4ul droplets of varying protein-to-precipitant ratios. To prepare a DMO-non-heme iron-dicamba crystal, some crystals were transferred to a cryo-amenable storage solution that contained 25 mM dicamba (12.3 % PEG6000, 95 mM sodium acetate pH 5.5, 21% glycerol, 1mM NaN3, and 25 mM dicamba) for 5-6 hours prior to plunge-cooling for cryo-storage and low temperature data collection. VAPOR DIFFUSION, SITTING DROP, temperature 294K

Crystal Structure of Dicamba Monooxygenase with Non-heme Cobalt and Dicamba

Crystal Structure of Dicamba Monooxygenase with Non-heme Cobalt and DCSA

Crystal Structure of Dicamba Monooxygenase with Non-heme Iron

MR was performed using a preliminary DMO structure. This early DMO structure was obtained largely using a high-redundancy, 1.5418 A wavelength data set for Fe single wavelength anomalous dispersion (SAD) phasing, with assistance from the sulfur anomalous signal in a high-redundancy, 2.29 A wavelength data set.

Rieske non-heme iron oxygenase, ELECTRON TRANSPORT, OXIDOREDUCTASE