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
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
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
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
purified recombinant enzyme, vapour diffusion method, 10 mg/ml protein in 20 mM HEPES, pH 6.8, 0.5 M NaCl, 1 mM DTT, and 0.5 mM EDTA, is mixed with an equal volume of reservoir solution containing 0.1 M MES, pH 6.0, 35% v/v 2-methyl-2,4-pentanediol, and 0.2 M LiSO4, equilibration against 1 ml of mother liquor, room temperature, 6 weeks, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified native and selenomethionine-labeled recombinant enzyme, hanging drop vapour diffusion method, 18°C, 2.5 mg/ml protein in 50 mm HEPES, pH 7.0, 5 mM Tris, pH 8.0, 0.15 mM ammonium sulfate, 6% PEG 4000, 0.1 M NaCl, 0.5 mM EDTA, and 0.5 mM DTT, mixed with reservoir solution containing 1 M HEPES, pH 7.0, 0.3 M ammonium sulfate, and 12% PEG 4000, plus 1 mM NADPH, X-ray diffraction structure determination and analysis at 2.3 A resolution