EC Number   |
|---|
    1.4.1.16 | apo form and in complex with meso-diaminopimelate, D-leucine, and 4-methyl-2-oxopentanoic acid, sitting drop vapor diffusion method, using MES (0.1 M, pH 6.0), 15% (w/v) PEG 20000, and 5% (v/v) glycerol |
| 1.4.1.16 | apo form and in complex with NADP+ and both NADPH and meso-2,6-diaminoheptanedioate, sitting drop vapor diffusion method, using 0.1m HEPES buffer (pH 7.5) with 30% 2-methyl-2,4-pentanediol and 5% (v/v) glycerol |
| 1.4.1.16 | apo form and in complex with NADP+ and N-tris(hydroxymethyl)methyl-2-aminoethanesulfonic acid, sitting drop vapor diffusion method, using 1.9 M ammonium sulfate,0.1 M Tris-HCl pH 7.5 |
| 1.4.1.16 | crystallization in the presence of NADP+, only monoclinic crystals are suitable for X-ray diffraction, 2.2 A resolution |
| 1.4.1.16 | crystals of the ternary complex formed from the enzyme, NADP+ and the inhibitor (2S,5S)-2-amino-3(3-carboxy-2-isoxazolin-5-yl)propanoic acid |
| 1.4.1.16 | crystals of the ternary complex formed from the enzyme, NADP+ and the inhibitor L-2-amino-6-methylene-pimelate, 2.1 A resolution |
| 1.4.1.16 | enzyme-NADP+ complex, hanging drop vapour diffusion, crystals of maximum dimensions of 0.05 x 0.05 x 0.5 mm are observed in 1 M ammonium sulfate, 1.2 M lithium sulfate, 100 mM HEPES, pH 7.5, crystals of dimensions 0.3 x 0.05 x 0.5 mm are obtained from 13-17% polyethylene glycol 8000 in 100 mM sodium cacodylate, pH 6.5 and 150-300 mM Mg(OAc)2 |
| 1.4.1.16 | molecular docking of substrates meso-DAP and pyruvic acid to wild-type and mutant R71A. Substrate binding with meso-DAP or pyruvic acid changes the rigidity of the enzyme and the secondary structure around R71 |
