EC Number |
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4.4.1.21 | Co2+-substituted BsLuxS is cocrystallized with inhibitors (2S)-2-amino-4-[(2R,3S)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid and (2S)-2-amino-4-[(2R,3R)-2,3-dihydroxy-3-N-hydroxycarbamoylpropylmercapto] butyric acid by the hanging drop vapor diffusion method |
4.4.1.21 | hanging drop vapor diffusion, inactive mutant C84A of Co2+-substituted LuxS is cocrystallized with the 2-ketone intermediate and the structure is determined to 1.8 A resolution |
4.4.1.21 | hanging-drop vapor diffusion method with ammonium sulfate as precipitant, structure at 1.6 A resolution |
4.4.1.21 | hanging-drop vapour diffusion method with ammonium sulfate as the precipitant. The crystals belong to the enantiomorphic space groups P6(1)22 or P6(5)22 with approximate unit-cell parameters A = b = 63.6, c = 151.5 A. The crystals diffract X-rays to at least 1.55 A resolution on a synchrotron-radiation source |
4.4.1.21 | purified recombinant enzyme, hanging-drop vapour-diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 10 mM Tris-HCl pH 8.0, 100 mM NaCl, 1 mM DTT, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl pH 8.0, 20% w/v PEG 3350, and equilibartion against 0.2 ml of reservoir solution, 18°C, X-ray diffraction structure determination and analysis at 2.4 A resolution |
4.4.1.21 | structure of LuxS is determined at 1.2 A resolution, together with the binary complexes of LuxS with S-ribosylhomocysteine and homocysteine to 2.2 A and 2.3 A resolution, hanging-drop vapour diffusion method |
4.4.1.21 | to 1.93 A resolution |