Proteins of the Bacillus stearothermophilus ribosome. Crystallization of proteins L30 and S5

J Biol Chem. 1983 Nov 10;258(21):13328-30.

Abstract

Proteins L30 and S5 from the 50 S and 30 S subunits, respectively, of the Bacillus stearothermophilus ribosome have been crystallized. L30 crystals are tetragonal and the space group is P4(1)2(1)2 (or P4(3)2(1)2) with cell dimensions a = b = 46.3 A and c = 61.4 A. S5 crystals are trigonal with the space group P3(1)21 (or P3(2)21) and cell dimensions a = b = 59.3 A and c = 109.8 A. In both cases, there appears to be a single molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Geobacillus stearothermophilus / analysis*
  • Protein Conformation
  • Ribosomal Proteins / isolation & purification*
  • Ribosomes / analysis*
  • X-Ray Diffraction

Substances

  • Ribosomal Proteins
  • ribosomal protein L30
  • ribosomal protein S5