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6.1.1.12: aspartate-tRNA ligase

This is an abbreviated version!
For detailed information about aspartate-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.12

Reaction

ATP
+
L-aspartate
+
tRNAAsp
=
AMP
+
diphosphate
+
L-aspartyl-tRNAAsp

Synonyms

Antigen T5, AsnRS, Asp-RS, ASPA, Aspartate--tRNA ligase, Aspartic acid translase, Aspartyl ribonucleate synthetase, Aspartyl ribonucleic synthetase, aspartyl ribonuleic synthetase, Aspartyl-transfer ribonucleic acid synthetase, Aspartyl-transfer RNA synthetase, Aspartyl-tRNA synthetase, AspRS, AspS, Bt cyt-AspRS, cytoplasmic aspartyl-tRNA synthetase, D-AspRS, DARS2, discriminating aspartyl-tRNA synthetase, discriminating AspRS, DRS, Drs2, Ec AspRS, HS cyt-AspRS, Hs mt-AspRS, hsAspRS, IBI1, mAspRS, mitochondrial aspartyl-tRNA synthetase, mmAspRS, mt-AspRS, non-discriminating aspartyl-tRNA synthetase, non-discriminating AspRS, Pa AspRS, Synthetase, aspartyl-transfer ribonucleate, Tb-AspRS1, Tb-AspRS2, TK0492

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.12 aspartate-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.12 - aspartate-tRNA ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of aspartyl-tRNA synthetase is determined at 2.8 A resolution
analysis of the 2.6-A resolution crystal structure of Escherichia coli AspRS with bound aspartyl-adenylate, AspAMP, molecular dynamics simulations
of enzyme complexed with its cognate tRNA
-
purified recombinant enzyme, in ammonium sulfate, NaCl, bis Tris propane, isopropanol, X-ray diffraction structure determination at 2.7 A resolution and structure analysis
-
hanging drop vapor diffusion method, in 30% (w/v) PEG 4000, 100 mM ammonium sulfate, 100 mM sodium citrate at pH 5.6
-
hanging drop vapor diffusion method, using 7% (w/v) PEG 4000, 0.1 M ammonium sulfate, 0.1 M sodium citrate pH 5.6
vapor diffusion method, using 10% (m/v) PEG-3350 and 0.5M of ammonium sulfate in 25 mM Bis-Tris pH 5.5
sitting drop vapor diffusion method, using 30% (v/v) pentaerythritol ethoxylate, 0.1 M magnesium formate, 0.1 M Tris-HCl, pH 8.5
-
binary complex formed by the enzyme and tRNAAsp
-
purified recombinant truncated enzyme, tri- and tetragonal crystals, X-ry structure determination at 3 and 2.3 A resolution, respectively, molecular replacement, structure analysis and modeling
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
-
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
-
at 2.5 A resolution
-
enzyme complexed with a non-hydrolysable analogue of asparaginyl-adenylate and with ATP, X-ray diffraction structure determination at 2.6 A resolution
-
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
-
isozyme AspRS2, hanging-drop vapour diffusion method, pH 9.5, in presence of PEG 8000 and NaCl, structure determination
-
purified enzyme complexed with tRNAAsp from Thermus thermophilus or Escherichia coli, potential intermediate of the recognition process, protein solution: 15 mg/ml of enzyme, 7.35 mg/ml of tRNA, plus equal volume of reservoir solution: 10 mM MgCl2, 50 mM HEPES, pH 7.5, 0.7 M sodium citrate, 17°C, 2 weeks, X-ray diffraction structure determination at 3.5 A resolution, structure analysis
-
purified recombinant enzyme, hanging-drop vapour diffusion method, in presence of PEG 8000, at 293K, growth kinetics and solubility measurements, X-ray diffraction structure determination at 3.1 A resolution
-
purified wild-type and seleno-Met isozymes AspRS2, vapour phase diffusion from mother liquid: 100 mM CHES buffer, pH 9.5, 200 mM NaCl, 10% w/v PEG 8000, X-ray diffraction structure determination at 2.3 A resolution, structure analysis
-