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1-Cys type selenoprotein MsrA at 1.6â1.8 A, including the reduced, oxidized (sulfenic acid), and substrate-bound forms. The overall structure folds into a catalytic domain and a helical domain absent from other known MsrA structures. The side chain length of residue Glu55 is critical for its proton donor function
structure of dimeric MsrA to 2.9 A resolution, having the dimer interface around the two catalytic Cys16 residues. A central cone-shaped hole is present in the surface model of dimeric structure, and the two Cys16 residues constitute the base of the hole
molecular modeling. The conserved residue Glu99 is buried in the Met-S-(O) groove, which might contribute to the correct placing of substrates. Residue Asp134 does not form hydrogen bonds with the substrates but only within the enzyme
15-50 mg/ml purified recombinant MsrA in 50 mM Tris-HCl, pH 8.0, 2 mM EDTA, and 10 mM DTT, hanging drop vapour diffusion method, droplet size is 0.004-0.008 ml, equal volumes of protein and precipitant solution, X-ray diffraction structure determination and analysis at 1.9 A resolution
single crystals of recombinant N-terminally 10His-tagged enzyme MsrA complexed with protein-bound methionine, hanging drop method, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 1 mM EDTA, 1 mM tris(carboxyethyl)phosphine hydrochloride, precipitant solution contains 2.0 M sodium formate, 0.1 M sodium citrate, pH 6.0, 4Â°C, 1 week, prior to data collection, crystals are soaked in 6.3 M sodium formate, 0.1 M sodium citrate, pH 6.0, for 2 min, and are flash-cooled, X-ray diffraction structure determination and analysis at 1.5 A resolution, polycrystalline clusters are obtained by sitting drop vapor diffusion method
crystals are obtained using the microbatch-under-oil method, four structures of the MsrA domain of the PilB protein from Neisseria meningitidis, representative of four catalytic intermediates of the MsrA catalytic cycle, are determined by X-ray crystallography