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We describe the high resolution structure of the large ribosomal subunit from Deinococcus radiodurans (D50S), a gram-positive mesophile suitable for binding of antibiotics and functionally relevant ligands. The over-all structure of D50S is similar to that from the archae bacterium Haloarcula marismortui (H50S); however, a detailed comparison revealed(More)
copy (cryo-EM) have also revealed new features of ribo-somal particles and their complexes (Gabashvili et al., 1999b, 2000; Stark et al., 2000). In parallel, the structures of several ribosomal protein–RNA complexes have been determined at high resolution (Conn et al. Structure The small ribosomal subunit from T. thermophilus 22603 Hamburg contains 19(More)
Despite the appearance of bacterial strains resistant to all clinical antibiotics, including vancomycin (the 'last resort'), development of new antimicrobial agents has slowed during recent decades. To aid design of new antibiotics, we must develop a detailed understanding of the mechanisms of antibiotic action and antibiotic resistance. Several classes of(More)
BACKGROUND The bacterial ribosome is a primary target of several classes of antibiotics. Investigation of the structure of the ribosomal subunits in complex with different antibiotics can reveal the mode of inhibition of ribosomal protein synthesis. Analysis of the interactions between antibiotics and the ribosome permits investigation of the specific(More)
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