Thermus thermophilus ribosomes for crystallographic studies.
Three-dimensional crystals of the 70S ribosomes, the 70S ribosome-mRNA-tRNA complex, the 30S ribosomal subunits, several ribosomal proteins, the elongation factor G and threonyl- and seryl-tRNA synthetases from a Gram-negative extreme thermophilic bacterium, Thermus thermophilus, have been obtained at our institute. X-ray and neutronographic data from the 70S ribosome crystals have been collected up to 18 A and 60 A, respectively. Two-dimensional crystalline sheets of the 70S ribosomes have been studied by electron microscopy. Structural studies of crystals of 2 ribosomal proteins, L1 and S6, elongation factor G and threonyl- and seryl-tRNA synthetases are also in progress. At present, Thermus thermophilus seems to be the most suitable microorganism to isolate ribosomes and their constituents for crystallographic studies.
Yusupov
M M
MM
Institute of Protein Research, Academy of Sciences of the USSR, Moscow.
Garber
M B
MB
Vasiliev
V D
VD
Spirin
A S
AS
D001426:Bacterial Proteins / Q000737:chemistry; D001483:Base Sequence; D003461:Crystallography; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009502:Neutrons; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D012329:RNA, Bacterial / Q000737:chemistry; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000235:genetics; D012269:Ribosomal Proteins / Q000737:chemistry; D012270:Ribosomes / Q000737:chemistry* / Q000648:ultrastructure; D016963:Thermus thermophilus / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012336:RNA, Ribosomal, 16S; D012269:Ribosomal Proteins