EC Number   |
|---|
    6.3.1.1 | at 2.7 A resolution |
| 6.3.1.1 | crystal structure of native AsnA and complexed with L-asparagine and AMP at 2.5 A, 2.2 A and 2.2 A resolution, respectively |
| 6.3.1.1 | crystallized in two different conditions using the hanging-drop vapour-diffusion method. Crystals belonging to space group C2 with unit-cell parameters a = 103.6, b = 43.3, c = 121.5 A, beta = 112.6° and one dimer per asymmetric unit are obtained in the presence of 2-propanol and PEG 4000 at pH 5.6. Another crystal form is obtained in the presence of dioxan and belongs to the monoclinic space group P2(1), with unit-cell parameters a = 96.8, b = 103.9, c = 98.4 A, beta = 107.5° and two dimers per asymmetric unit. Two different native diffraction data sets are collected to 2.3 A and 3.0 A resolution using synchrotron radiation and cryocooling for crystals belonging to space groups C2 and P2(1), respectively |
| 6.3.1.1 | purified recombinant His6-tagged apoenzyme, hanging drop vapor diffusion method, mixing of 0.001 ml of 73 mg/ml protein in 50 mM Tris-Cl, 200 mM NaCl, and 10 mM 2-mercaptoethanol, pH 7.5, with 0.001 ml of reservoir solution containing 0% w/v PEG 20000, 20% v/v PEG monomethyl ether 550, 0.03 M NPS (sodium nitrate, disodium hydrogen phosphate, ammonium sulfate), and 0.1 M MOPS/HEPES-Na, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, modeling |
| 6.3.1.1 | sitting-drop vapor diffusion. The fold of this protein is similar to that of bacterial asparagine synthetase A and resembles the catalytic cores of aspartyl-tRNA synthetase and asparaginyl-tRNA synthetase |
