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Results 1 - 7 of 7
EC Number Crystallization (Commentary)
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12purified MoaB, sitting drop vapour diffusion method, 0.001 ml of 11 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, are mixed with 0.001 ml of well solution containing 20% w/v PEG 3350, and 0.2 M tripotassium citrate monohydrate, 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 1.64 A resolution
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12purified recombinant apo form molybdopterin synthase and molybdopterin synthase-precursor Z complex using wild-type and mutant K126A MoeE, X-ray diffraction structure determination and analysis, structure modeling with the enzyme from Staphylococcu aureus, overview
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12purified recombinant enzyme, vapor diffusion, protein in M NaCl, 0.1 M HEPES, pH 7.5, is mixed with mother liquor containing 20% v/v glycerol, X-ray diffraction structure determination and analysis at 1.45 A resolution
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12purified recombinant His-tagged apo form molybdopterin synthase and molybdopterin synthase-precursor Z complex using wild-type and mutant K123A MoeE, 10 mg/ml protein in a buffer containing 50 mM Tris-HCl, pH 8.0, and 50 mM NaCl, mixed with a precipitant consisting of 2.0 M sodium formate and 0.1 M sodium acetate, pH 5.3, at 22°C, 2 days, for the enzyme complex with precursor Z, 18% w/v PEG 8000, 0.1% polyvinylpyrrollidone K15, and 0.1 M Tris-HCl, pH 8.0, at 4°C is used, X-ray diffraction structure determination and analysis at 2.0 A resolution for the apoenzyme and at 2.5 A resolution for the enzyme complex, molecular replacement with MOLREP, modeling using the cyrstal structure of the Escherichia coli MPT synthase, overview
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12purified recombinant MoaE, MoaD, and mutant MoeE E141DELTA, the MoaD-MoeB complex is crystallized using 1.1 M (NH4)2SO4 and 0.1 M HEPES, pH 7.5, as precipitant at a protein concentration of 15 mg/ml within 4-8 months, MoeE mutant E141DELTA at a protein concentration of 20 mg/ml is crystallized from a solution containing 600 mM sodium formate, 15% polyethylene glycol 4000, 10% isopropyl alcohol, and 100 mM Tris, pH 7.5, within 2-3 days, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12structure at 2.1 A resolution. The overall structure is hetero-tetrameric, consisting of a MoaE2 dimer flanked on either side by single MoaD2 subunits. The carboxyl-terminal domain of MoaD2 inserted into MoaE2, forming the active pocket
Show all pathways known for 2.8.1.12Display the word mapDisplay the reaction diagram Show all sequences 2.8.1.12structure at 2.6 A resolution. The overall structure is hetero-tetrameric, consisting of a MoaE2 dimer flanked on either side by single MoaD2 subunits. The carboxyl-terminal domain of MoaD2 inserted into MoaE2, forming the active pocket
Results 1 - 7 of 7