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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems.

Thermus thermophilus tRNAAsp, purified from a non-recombinant source, has been crystallized in a complex with its cognate dimeric (alpha2) aspartyl-tRNA synthetase. Crystals diffract to 2.9 A resolution and belong to space group P63 with cell parameters a = b = 258, c = 90.9 A. The crystals contain one aspartyl-tRNA synthetase dimer and two tRNA molecules in the asymmetric unit, corresponding to a Vm of 4.85 A3 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.[1]

References

  1. Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems. Briand, C., Poterszman, A., Mitschler, A., Yusupov, M., Thierry, J.C., Moras, D. Acta Crystallogr. D Biol. Crystallogr. (1998) [Pubmed]
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