Proteins of the Bacillus stearothermophilus ribosome. Crystallization of proteins L30 and S5.
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.
D003460:Crystallization; D001411:Geobacillus stearothermophilus / Q000032:analysis*; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D012270:Ribosomes / Q000032:analysis*; D014961:X-Ray Diffraction
D012269:Ribosomal Proteins; C035201:ribosomal protein L30; C030831:ribosomal protein S5