A high resolution diffracting crystal form of the complex between yeast tRNAAsp and aspartyl-tRNA synthetase

J Mol Biol. 1988 May 5;201(1):235-6. doi: 10.1016/0022-2836(88)90450-0.

Abstract

Three new crystal forms of the complex between yeast tRNAAsp and aspartyl-tRNA synthetase have been produced. The best crystals, obtained after modifying both purification and crystallization conditions, belong to space group P2(1)2(1)2(1) and diffract to 2.7 A. Unit cell parameters are a = 210.4 A, b = 145.3 A and c = 86.0 A (1 A = 0.1 nm), with one dimeric enzyme and two tRNA molecules in the asymmetric unit.

MeSH terms

  • Amino Acyl-tRNA Synthetases / metabolism*
  • Aspartate-tRNA Ligase / metabolism*
  • Crystallization
  • RNA, Fungal / metabolism*
  • RNA, Transfer, Amino Acid-Specific / metabolism*
  • RNA, Transfer, Asp / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • X-Ray Diffraction

Substances

  • RNA, Fungal
  • RNA, Transfer, Amino Acid-Specific
  • RNA, Transfer, Asp
  • Amino Acyl-tRNA Synthetases
  • Aspartate-tRNA Ligase