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EC Number	Crystallization (Commentary)
2.3.1.136	OatWY is crystalised with bound substrate acetyl-CoA and its analogs (CoA, S-(2-oxopropyl)-CoA) using the hanging drop vapor diffusion technique. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. A significant movement of Tyr-171 blocks the active site of the enzyme in its native form
2.3.1.136	purified engineered apo-NeuO, a protein variant with four N-terminal RLKTQDS heptads, sitting drop vapour diffusion, 6.3 mg/ml protein in 10 mM Tris-HCl pH 7.5 and 150 mM NaCl, mixed with precipitant solution containing 0.1 M Tris, pH 7.2, 0.45 M glycine, 0.2 M NH4NO3, 7% PEG 4000 w/v, 1 week, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement

EC Number

Crystallization (Commentary)

2.3.1.136

OatWY is crystalised with bound substrate acetyl-CoA and its analogs (CoA, S-(2-oxopropyl)-CoA) using the hanging drop vapor diffusion technique. The structure of OatWY reveals an intimate homotrimer of left-handed beta-helix motifs that frame a deep active site cleft selective for the polysialic acid-bearing substrate. A significant movement of Tyr-171 blocks the active site of the enzyme in its native form

2.3.1.136

purified engineered apo-NeuO, a protein variant with four N-terminal RLKTQDS heptads, sitting drop vapour diffusion, 6.3 mg/ml protein in 10 mM Tris-HCl pH 7.5 and 150 mM NaCl, mixed with precipitant solution containing 0.1 M Tris, pH 7.2, 0.45 M glycine, 0.2 M NH4NO3, 7% PEG 4000 w/v, 1 week, 20°C, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement

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Release 2023.1 (January 2023)