EC Number |
---|
1.1.1.100 | - |
1.1.1.100 | apo-form complexed with NADPH, vapor diffusion method, using 10% (w/v) polyethylene glycol 4000, 10% (v/v) 2-propanol, 0.1 M HEPES pH 7.0 and 30% (v/v) jeffamine ED2001, 0.1 M HEPES pH 7.5 |
1.1.1.100 | at 2.4 A resolution, space group P21 with unit-cell parameters a = 70.6, b = 120.7, c = 136.4 and beta = 104.4. The structure contains two tetramers displaying 222 symmetry (all chains are completely traced, although for some chains the electron density for residues 189-203 is poor) and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates |
1.1.1.100 | crystalized at a resolution of 2.25 A |
1.1.1.100 | diffraction to 1.8 A, determinantion of initial phases by molecular replacement |
1.1.1.100 | diffraction to 2.4 A. Final model contains two tetramers displaying 222 symmetry and 575 water molecules in the crystallographic asymmetric unit, but no bound cofactors or substrates |
1.1.1.100 | hanging drop vapor diffusion method, apoenzyme is crystallized by using 100 mM Na-HEPES (pH 7.5), 30% (w/v) PEG 400 and 200 mM magnesium chloride hexahydrate, while the complex with NADP+ is crystallized by using 200 mM sodium citrate tribasic dehydrate and 20% (w/v) PEG 3350 |
1.1.1.100 | hanging drop vapor diffusion method, using 2.0-2.7 M ammonium sulfate and 0.1 M Tris (pH 9.0) |
1.1.1.100 | high-resolution crystal structures of the enzyme (MabA) in its apo, NADP+-bound and NADPH-bound forms. Crystals are grown in sitting drops in MR Crystallization Plates (Hampton Research) at 18°C |
1.1.1.100 | in complex with hexanoyl-CoA, hanging drop vapor diffusion method, using |