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purified His-tagged enzyme in complex with acetate or urea, mixing of 13 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with PEG448-49, 250 mM urea, pH 4.0, and 20% v/v glycerol in capillaries using the counter-diffusion technique, 20Â°C, X-ray diffraction structure determination and analysis at 1.78 A and 2.15 A resolution, respectively
hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 M sodium cacodylate and 18% (w/v) PEG 8000 pH 6.2 for the native protein or 18% (w/v) PEG 8000, 0.2 M calcium acetate and 0.1 M sodium acetate pH 5.8 for the SeMet-substituted protein
crystal structure of AmiF is solved to 1.75 A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture characteristic of the nitrilase superfamily
after incubation at the optimal temperature for activity of the enzyme (50Â°C) for 40 h, the enzyme maintains around 95% of its initial activity. Activity is gradually lost when the enzyme is incubated at temperatures over 65Â°C for 30 min. The melting temperature is at 73.5Â°C
The effect of growth in continuous culture at various input C:N ratios on the expression of proteins involved in the transport and metabolism of methanol and short-chain amides by Methylophilus methylotrophus
Borges, C.L.; Pereira, M.; Felipe, M.S.; de Faria, F.P.; Gomez, F.J.; Deepe, G.S.; Soares, C.M.
The antigenic and catalytically active formamidase of Paracoccidioides brasiliensis: protein characterization, cDNA and gene cloning, heterologous expression and functional analysis of the recombinant protein