Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli

Protein Sci. 1997 Dec;6(12):2636-8. doi: 10.1002/pro.5560061217.

Abstract

Arginyl-tRNA Synthetase, a class I aminoacyl tRNA synthetase playing a crucial role in protein biosynthesis, has been crystallized for the first time. Polyethylene glycol (PEG) was used as a precipitant, and the crystallization proceeded at pH 6.5. These single crystals diffracted to 2.8 A with a rotating anode X-ray source and R-axis IIc image plate detector. They have an orthorhombic space group P2(1)2(1)2 with unit cell parameters of a = 251.51 A, b = 53.12 A, and c = 52.35 A. A complete native data set has been collected at 3.1 A resolution for these crystals.

MeSH terms

  • Arginine-tRNA Ligase / chemistry*
  • Chemical Precipitation
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Polyethylene Glycols

Substances

  • Polyethylene Glycols
  • Arginine-tRNA Ligase