EC Number   |
|---|
    6.1.1.4 | cocrystallizations with each of the tRNALeu isoacceptors are attempted. Cocrystals are obtained by the hanging-drop vapour-diffusion method, but only when the tRNALeu isoacceptor with the anticodon CAA is used. Electrophoretic analyses reveals that the crystals contain both leucyl-tRNA synthetase and tRNALeu, suggesting that they are LeuRS-tRNALeu complex crystals. A data set diffracting to 3.3 A resolution is collected from a single crystal at 100 K. The crystal belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 118.18, b = 120.55, c = 231.13 A |
| 6.1.1.4 | construction of a structural model of the completely solvated leucyl-tRNA synthetase complexed with valyl-tRNALeu |
| 6.1.1.4 | crystal and cocrystal structures for LeuRS, IleRS, and ValRS suggests that the CP1 domain rotates via its flexible beta-strand linkers relative to the main body along various steps in the enzymes reaction pathway. Computational analysis suggested that the end of the N-terminal beta-strand acted as a hinge. A molecular hinge might specifically direct movement of the CP1 domain relative to the main body |
| 6.1.1.4 | crystal growth in presence of mercuric chloride, soaking of the crystals in solution containing 0.6 mM of the non-hydrolyzable substrate analogue norvaline-AMS for 1 month, or cocrystallization of enzyme and norvaline-AMS, X-ray diffraction structure determinationat 2.0-2.2 A resolution and analysis |
| 6.1.1.4 | crystal structure of editing domain of Escherichia coli LeuRS in both apo form and complexes with methionine and isoleucine at 2.0 A, 2.4 A, and 3.2 A resolution, hanging drop vapour diffusion method |
| 6.1.1.4 | crystal structure of leucyl-tRNA synthetase complexed with tRNALeu in the post-transfer-editing conformation, crystals of the complex are grown at 20°C by hanging drop vapour diffusion |
| 6.1.1.4 | crystallization of enzyme alone or in complex with leucine or leucyl-adenylate analogue, and crystallization of selenomethionine-enzyme, hanging-drop vapour-diffusion method with ammonium sulfate as precipitant, X-ray diffraction structure determination at 1.9-6 A resolution |
| 6.1.1.4 | enzyme LeuRS mutant T252A in a complex with tRNALeu and leucyl-adenylate sulphamoyl analogue (Leu-AMS), both positioned in the synthetic active site, and Leu2AA located in the editing domain, X-ray diffraction structure determination and analysis at resolution, replacement using structure PDB ID 4AQ7, modeling |
| 6.1.1.4 | hanging drop vapor diffusion method, using 0.1 M bis-Tris (pH 5.5), 0.6 M ammonium acetate, and 20% (w/v) PEG3350 at 4°C |
| 6.1.1.4 | hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = b = 186.20, c = 91.43 A, alpha = beta = 90, gamma = 120°. The asymmetric unit contains one molecule of LeuRS, with a corresponding crystal volume per protein weight of 3.2 A3 Da(-1) and a solvent content of 60.7%. A data set diffracting to 2.2 A resolution is collected from a single crystal at -173°C. Selenomethionine-substituted protein crystals are prepared in order to solve the structure by the SAD phasing method |
