Characterization and preliminary crystallographic studies on large ribosomal subunits from Thermus thermophilus.

摘要: Diffracting crystals, suitable for X-ray crystallographic analysis, have been obtained from large (50 S) ribosomal subunits Thermus thermophilus. These with P41212 symmetry and a unit cell of 495 A × 196 A, reach typically size 0·15 mm 0·25 0·35 mm. Using synchrotron radiation at cryo-temperature, these crystals diffract X-rays to better than 9 resolution, do not show any measurable decay after few days irradiation. They complete series grown by us, particles the same source, including 30 S subunits, 70 ribosomes complexes latter with: (1) an oligomer 35 uridine residues (2) oligonucleotide together approximately two Phe-tRNAPhe molecules. Crystallographic analysis various members this should provide information investigating conformational changes that take place upon association their as well binding non-ribosomal components participate in protein biosynthesis.