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Results 1 - 2 of 2
EC Number Crystallization (Commentary) Reference
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116seleno-L-methionine-substituted wild-type or N-terminally truncated mutant enzymes, hanging drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM Tris, pH 7.4, 1 mM MnCl2, and 5 mM DTT, with crystallization solution containing 0.1 M phosphate citrate, pH 4.2, 10% w/v PEG 3000, 0.2 M NaCl or with 0.1 M HEPES, pH 7.5, 7% w/v PEG 8000, 8% v/v ethylene glycol, 22°C, X-ray diffraction structure determination and analysis at 3.30 A resolution, molecular replacement, molecular modeling 734179
Show all pathways known for 3.5.1.116Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.116wild-type enzyme and mutant E183A complexed with substrate, reaction intermediate, and product, sitting drop vapor diffusion method, mixing of 10 mg/ml protein in 50 mM Tris, pH 7.4, 1 mM MnCl2, and 5 mM DTT, with crystallization buffer of 0.1 M 4-morpholineethanesulfonic acid, pH 6.5, and 12% w/v PEG 20000, at 22°C, crystals of the AtUAH binary complex with substrate or reaction intermediate by co-crystallization of mutant E183A with a (S)-ureidoglycolate, from a crystallization solution containing 0.2 M calcium acetate hydrate, 20% w/v PEG 3350, 1 mM MnCl2, and 5 or 2 mM, respectively, (S)-ureidoglycolate, X-ray diffraction structure determination and analysis at 1.45-2.20 A resolution 734481
Results 1 - 2 of 2