1.1.1.100	-	285681, 285682	
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	740558	
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	706640	
1.1.1.100	crystalized at a resolution of 2.25 A	723843	
1.1.1.100	diffraction to 1.8 A, determinantion of initial phases by molecular replacement	684165	
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	689973	
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	740023	
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)	740630	
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	762566	
1.1.1.100	in complex with hexanoyl-CoA, hanging drop vapor diffusion method, using	740013	
1.1.1.100	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	669470	
1.1.1.100	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	667520	
1.1.1.100	sitting drop vapor diffusion method, using 15-18% (w/v) PEG3350 and 0.4 M ammonium acetate in sodium acetate buffer at pH 5.0	741044	
1.1.1.100	structure determination and similarities within short-chain alcohol dehydrogenase family, catalytic mechanism	285683	
1.1.1.100	vapor diffusion method, using 0.1 M MES (pH 7.1), 1.6 M ammonium sulfate, and 10% (w/v) 1,4-dioxane	739901