EC Number   |
|---|
    4.1.2.4 | - |
| 4.1.2.4 | crystals of native wild-type enzyme and SeMet enzyme are grown by vapor-diffusion sitting drop method, analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99 A resolution |
| 4.1.2.4 | hanging drop vapor diffusion method |
| 4.1.2.4 | hanging drop vapor diffusion method, crystal structures of full length and C-terminal truncated enzyme is determined at 2.8 A resolution. Both contain the typical (alpha/beta)8 TIM-barrel fold of class I aldolases. C-terminal truncation resulting in missing the last alpha9 and beta8 secondary elements, allows the enzyme to maintain activity comparable to the full length enzyme. Arg186 and Ser205 residues at the C-terminus appear mutually supplemental or less indispensible for substrate phosphate moiety recognition |
| 4.1.2.4 | hanging drop vapour diffusion method with 20% (w/v) polyethylene glycol 1000, 0.2 M zinc acetate, and 0.1 M acetate buffer (pH 4.5) |
| 4.1.2.4 | microbatch method, crystal structure of the enzyme and its complex with 2-deoxy-D-ribose 5-phosphate |
