EC Number   |
|---|
    1.1.1.2 | - |
| 1.1.1.2 | 16°C, wild-type RADH: 15 mg/ml stock solution (21% polyethyleneglycol monomethyl ether 550, 0.1 M Tris-HCl, 50 nM MgCl2, 40 mM acetophenone, 10 mM NADP+), growth for 3 weeks, max. size 0.25 mm x 0.25 mm x 1.0 mm, RADH-G37D: 21 mg/ml stock solution (methyl-2,4-pentanediol, 20% polyethyleneglycol 400 or polyethyleneglycol monomethyl ether 550, 0.1 M Hepes, 50 mM MgCl2 59 mM 1-phenylethanol, 25 mM NADH), growth 1 week, max. size 0.4 mm x 0.5 mm x 1.7 mm |
| 1.1.1.2 | apo form |
| 1.1.1.2 | at 22°C by vapor-diffusion using the hanging drop method. ALR1 in ternary complex with the coenzyme NADPH and 3,5-dichlorosalicylic acid, at a resolution of 2.41 A |
| 1.1.1.2 | both in presence and absence of NADP+ |
| 1.1.1.2 | crystal structure of the enzyme in a binary complex with 5-hydroxy-NADP at 1.68 A resolution |
| 1.1.1.2 | crystals of D275PEhADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant D275P-EhADH1 suggests that a proline residue at position 275 thermostabilizes the enzymes by reducing flexibility and by reinforcing hydrophobic interactions at the dimerdimer interface of the tetrameric ADH |
| 1.1.1.2 | crystals of P275DTbADH1 are grown using the hanging-drop vapor-diffusion method at 20°C. Crystal structure of the thermostabilized mutant P275D-EhADH1 suggests that a proline residue at position 275 thermostabilizes the enzymes by reducing flexibility and by reinforcing hydrophobic interactions at the dimerdimer interface of the tetrameric ADH |
| 1.1.1.2 | hanging drop method, with NADPH, ammonium sulfate, Tris HCl-buffer, pH 8.1, buffer C, maximum side: 0.3 mm x 0.1 mm x 0,1 mm after 1 week |
| 1.1.1.2 | in complex with NADP+, to 3.2 A resolution. Crystals belong to space group P21 |
