EC Number |
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3.4.24.B20 | cytosolic region of apo-FtsH, microbatch method by mixing equal volumes of 20 mg/ml protein with crystallization buffer containing 30% w/v PEG 400, 200 mM CaCl2, 100 mM HEPES, pH 7.5, 200 mM glycine, and 0.1-0.2% w/v low-melt agarose, 20°C, X-ray diffraction structure determination and analysis at 2.6 A resolution |
3.4.24.B20 | structures of a transmembrane helix-lacking FtsH construct from Aquifex aeolicus, at 2.9 A and 3.3 A resolution in space groups R32 and P312, respectively. In both structures, the FtsH hexamer is created from two different subunits of the asymmetric unit by the threefold symmetry of the crystals. All subunits are loaded with ADP. Within the ATPase cycle while the whole subunit switches from the opened to the closed state, pore loop-1 interacts with the substrate and translocates it into the proteolytic chamber |
3.4.24.B20 | vapor diffusion method, using either 2 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 10 mM EDTA or, as another condition, 60% tacsimate pH 7.0, 10 mM adenylyl imidodiphosphate lithium salt hydrate |