Crystallization and preliminary X-ray diffraction data of the second and archaebacterial-type aspartyl-tRNA synthetase from Thermus thermophilus

Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1177-9. doi: 10.1107/s0907444901009611. Epub 2001 Jul 23.

Abstract

The archaebacterial-type aspartyl-tRNA synthetase (AspRS2) from the thermophilic eubacterium Thermus thermophilus was crystallized using the hanging-drop vapour-diffusion method. Crystals grew at pH 9.5 in the presence of PEG 8000 and NaCl. A native diffraction data set has been collected at 2.5 A resolution using synchrotron radiation and cryocooling. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 57.3, b = 121.9, c = 166.9 A and V(M) = 3.03 A(3) Da(-1). There is one dimer of M(r) 96 000 per asymmetric unit. A molecular-replacement analysis gave solutions for the rotation and translation functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaea / enzymology
  • Aspartate-tRNA Ligase / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Protein Conformation
  • Thermus thermophilus / enzymology*

Substances

  • Aspartate-tRNA Ligase