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EC Number	Crystallization (Commentary)
1.3.1.34	15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives
1.3.1.34	the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate

EC Number

Crystallization (Commentary)

1.3.1.34

15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives

1.3.1.34

the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate

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Release 2023.1 (January 2023)