Growth kinetics, diffraction properties and effect of agarose on the stability of a novel crystal form of Thermus thermophilus aspartyl-tRNA synthetase-1

Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):552-8. doi: 10.1107/s0907444901001743.

Abstract

Growth kinetics and diffraction properties of monoclinic crystals of eubacterial Thermus thermophilus aspartyl-tRNA synthetase-1 (AspRS-1) prepared in the presence of polyethylene glycol and agarose are studied. Their solubility and two-dimensional phase diagram are compared with those of orthorhombic crystals which grow in the presence of sodium formate or ammonium sulfate. The growth mechanism of the novel crystals was monitored by atomic force microscopy. The gel stabilizes the crystal lattice under the cryogenic conditions used for structure determination at high resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartate-tRNA Ligase / chemistry*
  • Aspartate-tRNA Ligase / metabolism*
  • Crystallization
  • Crystallography, X-Ray / methods
  • Enzyme Stability
  • Gels
  • Kinetics
  • Microscopy, Atomic Force
  • Osmolar Concentration
  • Sepharose / metabolism*
  • Solubility
  • Temperature
  • Thermodynamics
  • Thermus thermophilus / enzymology*

Substances

  • Gels
  • Sepharose
  • Aspartate-tRNA Ligase