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EC Number	Crystallization (Commentary)
2.6.1.17	diffration to 2.0 A resolution. The orthorhombic crystals contain one functional dimer in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal 5'-phosphate-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor pyridoxal 5'-phosphate covalently bound to the Lys232, although neither substrate nor cofactor has been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues
2.6.1.17	sitting drop vapour diffusion method, in the presence of 20% (w/v) PEG-3350, Tris-HCl (pH 8.5) and 200 mM MgCl2

EC Number

Crystallization (Commentary)

2.6.1.17

diffration to 2.0 A resolution. The orthorhombic crystals contain one functional dimer in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal 5'-phosphate-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor pyridoxal 5'-phosphate covalently bound to the Lys232, although neither substrate nor cofactor has been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues

2.6.1.17

sitting drop vapour diffusion method, in the presence of 20% (w/v) PEG-3350, Tris-HCl (pH 8.5) and 200 mM MgCl2

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Release 2023.1 (January 2023)