EC Number   |
Reference |
|---|
    4.2.1.33 | crystal structure isopropylmalate isomerase small subunit. Four molecules create an interlocked assembly with intermolecular disulfide linkages having a skewed 222 point-group symmetry. The structure reveals the formation of intermolecular disulfide linkages, and it provides insight into the dual substrate specificity of the enzyme |
722946 |
| 4.2.1.33 | sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol monomethyl ether 2000 and 0.1 MTris-HCl (pH 7.9) |
729127 |
| 4.2.1.33 | sitting-drop vapour-diffusion methodand hanging-drop vapour diffusion at 20°C, structures of oxidized and reduced forms of the large subunit of isopropylmalate isomerase (ox-MJ0499 and red-MJ0499, respectively) are reported at 1.8 and 2.7 A resolution, respectively. Significant large conformational changes are observed in the active site of red-MJ0499 when compared with ox-MJ0499 |
726596 |
| 4.2.1.33 | small subunit LeuD variants, X-ray diffraction structure determination and analysis at resolutions of 2.0 A for LeuD_1-156, 1.2 A for LeuD_1-168, and 2.5 A for LeuD_1-186, respectively |
716886 |
| 4.2.1.33 | variants LeuD-1-156 and LeuD-1-168, by sitting-drop vapour-diffusion method, crystals of LeuD-1-156 belong to the hexagonal system (space group P6122 or P6522) with up to four subunits in the asymmetric unit, whereas the crystals of LeuD-1-168 belong to the monoclinic system (space group P21) with two subunits in the asymmetric unit. Both crystals diffract to beyond 2.0 A resolution |
701510 |
