EC Number |
Reference |
---|
3.1.4.52 | BlrP1 is crystallized at 4°C in the dark using polyethyleneglycol in the presence of cyclic-di-GMP and Ca2+ |
713097 |
3.1.4.52 | crystals are grown by hanging-drop method at 18°C using 0.001 ml of protein solution mixed with an equal volume of reservoir solution, varying conditions using 0.1 M bis-Tris, pH 5.5, 0.2-0.4 M ammonium acetate, 25% w/v PEG 3350, with or without 20% v/v DMSO or 2.1 M DL-malic acid, pH 7.0, X-ray diffraction structure determination and analysis at 2.5 A resolution |
716096 |
3.1.4.52 | enzyme does not undergo global changes upon exposure to light. The chromophore environment of full-length enzyme is asymmetric |
682265 |
3.1.4.52 | purified recombinant detagged enzyme in complex with Fe2+, substrate cyclic di-3',5'-guanylate or final product GMP, hanging drop vapour diffusion method, mixing of equal volumes of 10 mg/ml protein with a precipitant solution made up of 0.1 M MES pH 6.5, 0.9 M succinic acid, and 2% PEG 2000, anomalous X-ray diffraction structure determination and analysis at 2.03-2.8 A resolution |
730416 |