Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase

Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1046-7. doi: 10.1107/s0907444999001468.

Abstract

Crystals of the 52 kDa monomeric Escherichia coli cysteinyl-tRNA synthetase complexed with ATP and cysteine have been grown by hanging-drop vapor diffusion from solutions containing ammonium sulfate as the precipitating agent. The crystals form long hexagonal rods in the space group P321 with unit-cell dimensions a = b = 82.3, c = 168.9 A. There is one enzyme molecule in the asymmetric unit. A complete native data set has been collected from a rotating-anode source to a resolution of 2.7 A at 103 K, with an Rmerge of 6.7%.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acyl-tRNA Synthetases / chemistry*
  • Amino Acyl-tRNA Synthetases / isolation & purification
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Protein Conformation

Substances

  • Bacterial Proteins
  • Amino Acyl-tRNA Synthetases
  • cysteinyl-tRNA synthetase