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Results 1 - 4 of 4
EC Number Crystallization (Commentary)
Show all pathways known for 1.14.14.155Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.155-
Show all pathways known for 1.14.14.155Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.155plate shaped crystals from 4.0 M sodium formate and 28% PEG 8000 in 0.2 M sodium acetate, X-ray analysis
Show all pathways known for 1.14.14.155Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.155purified recombinant N-terminally His6-tagged enzyme, by Microbatch crystallization, mixing of 7 mg/ml protein in 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor in a 1:1 ration, purified native enzyme, by vapour-diffusion technique, 10 mg/ml protein solution are mixed in equal volumes with 50 mM PIPES pH 6.5, 50% ammonium sulfate, room temperature, best from 100 mM HEPES pH 7.0, 20% PEG 3350 in the presence of 20 mM FMN, 5 mM NADH and 5 mM (-)-camphor, at 18°C, X-ray diffraction structure determination and analysis at 1.9-2.7 A resolution, the enzyme's crystal structure is solved by a combination of multiple anomalous dispersion from a bromine crystal soak and molecular replacement using a bacterial luciferase model
Show all pathways known for 1.14.14.155Display the word mapDisplay the reaction diagram Show all sequences 1.14.14.155vapour-diffusion technique, three-dimensional structures of the native enzyme and the FMN complex of the overexpressed form of the oxygenating component of the type II Baeyer-Villiger 3,6-diketocamphane monooxygenase have been determined to 1.9 A resolution
Results 1 - 4 of 4