Crystals of Thermus thermophilus tRNA Asp Complexed with its Cognate Aspartyl-tRNA Synthetase Have a Solvent Content of 75%. Comparison with Other Aminoacylation Systems - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Acta crystallographica Section D : Structural biology [1993-...] Année : 1998

Crystals of Thermus thermophilus tRNA Asp Complexed with its Cognate Aspartyl-tRNA Synthetase Have a Solvent Content of 75%. Comparison with Other Aminoacylation Systems

Résumé

Thermus thermophilus tRNA Asp , purified from a non-recombinant source, has been crystallized in a complex with its cognate dimeric (α2) aspartyl-tRNA synthetase. Crystals diffract to 2.9 Å resolution and belong to space group P 6 3 with cell parameters a = b = 258, c = 90.9 Å. The crystals contain one aspartyl-tRNA synthetase dimer and two tRNA molecules in the asymmetric unit, corresponding to a V m of 4.85 Å 3 Da −1 and 75% solvent content. When compared with those obtained for globular proteins these values are high, but fall within the range observed for other aminoacyl-tRNA synthetases, either free or complexed with their tRNAs. A comparative survey is presented here.

Dates et versions

hal-03611479 , version 1 (17-03-2022)

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Christophe Briand, Arnaud Poterszman, André Mitschler, Marat Yusupov, Jean-Claude Thierry, et al.. Crystals of Thermus thermophilus tRNA Asp Complexed with its Cognate Aspartyl-tRNA Synthetase Have a Solvent Content of 75%. Comparison with Other Aminoacylation Systems. Acta crystallographica Section D : Structural biology [1993-..], 1998, 54 (6), pp.1382-1386. ⟨10.1107/s0907444998005800⟩. ⟨hal-03611479⟩
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