Crystallization of a hyperthermophilic archaeal elongation factor 1 alpha

J Mol Biol. 1994 Sep 16;242(2):175-7. doi: 10.1006/jmbi.1994.1568.

Abstract

Intact and fully active elongation factor aEF-1 alpha from the hyperthermophilic archaeon Sulfolobus solfataricus has been crystallized as a complex with GDP. Crystals were stable at temperatures below 8 degrees C and showed significant diffraction beyond 3.0 A. The orthorhombic lattice parameters were a = 62.9 A, b = 81.3 A, c = 115.6 A with one molecule per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Chromatography, High Pressure Liquid
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / chemistry*
  • Sulfolobus / chemistry*

Substances

  • Bacterial Proteins
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors