EC Number   |
|---|
    6.1.1.12 | - |
| 6.1.1.12 | 7 different mutants, modification of crystal surfaces, investigation of crystallizability to determine the influence of surface residues and protein structure on crystal growth, packing arrangement, and quality |
| 6.1.1.12 | analysis of the 2.6-A resolution crystal structure of Escherichia coli AspRS with bound aspartyl-adenylate, AspAMP, molecular dynamics simulations |
| 6.1.1.12 | AspRS2, hanging drop vapour diffusion method, 0.002 ml of 14 mg/ml protein with 10% m/v PEG 8000, 200 mM NaCl, and 100 mM Na-CHES buffer, pH 9.5, X-ray diffraction structure determination and analysis at 2.3-3.2 A resolution |
| 6.1.1.12 | at 2.5 A resolution |
| 6.1.1.12 | binary complex formed by the enzyme and tRNAAsp |
| 6.1.1.12 | enzyme complexed with a non-hydrolysable analogue of asparaginyl-adenylate and with ATP, X-ray diffraction structure determination at 2.6 A resolution |
| 6.1.1.12 | hanging drop vapor diffusion method, in 30% (w/v) PEG 4000, 100 mM ammonium sulfate, 100 mM sodium citrate at pH 5.6 |
| 6.1.1.12 | hanging drop vapor diffusion method, using 7% (w/v) PEG 4000, 0.1 M ammonium sulfate, 0.1 M sodium citrate pH 5.6 |
| 6.1.1.12 | hanging-drop vapour-diffusion method, enzyme crystallizes either in a monoclinic or an orthorhombic habit. Minute amounts of protein impurities alter to a different extent the growth of each crystal form. The best synthetase crystals are obtained when the crystallizating solution is either enclosed in capillaries or immobilized in agarose gels |
