Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparative quantum mechanics/molecular mechanics and density functional theory calculations on the oxo-iron species. Protonation of the histidine ligands of iron is essential to reproduce the correct electronic representations of the enzyme. Enzyme is very efficient in reacting with substrates via low reaction barriers
density functional theory calculations based on a series of models for the key intermediate with the Fe(IV) ion coordinated by the expected two imidazoles from His99 and His255, two carboxylates, succinate and Asp101, and oxo ligands. Calculated parameters of distorted octahedral models for the intermediate, in which one of the carboxylates serves as a monodentate ligand and the other as a bidentate ligand, and a trigonal bipyramidal model, in which both carboxylates serve as monodentate ligands, agree well with the experimental parameters
electron spin echo-detected EPR spectrum ESE and deuterium electron spin echo envelope modulation spectrum ESEEM of the Fe(II)-NO form of the enzyme treated with 2-oxoglutarate and taurine
hanging drop vapor diffusion method, crystals of Escherichia coli TauD are grown in the presence of vanadyl, taurine, and the coproduct succinate yield a 1.73 A resolution structure containing two molecules in the asymmetric unit
three crystal structures of the apo form, vapor diffusion techniques, protein solution contains 1. 27-28 m/ml TauDPp in 25 mM Tris-HCl, pH 7.7, or 2. 21 mg/ml TauDPp in 25 mM Tris-HCl pH 7.7, containing 10 mM taurine, 0.1 M (NH4)2SO4 and 20% v?v glycerol, mixed with reservoir solution containing 1. 15% w?v PEG 1000, 40% v?v PEG 400, 0.15 M NaK phosphate, and 0.1 M imidazole chloride, pH 6.5, or 2. 20% w?v PEG 5000 monomethyl ether, 0.1 M Bis-Tris-HCl, pH 6.5, X-ray diffraction structure determination and analysis at 1.85-2.6 A resolution