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Science 29 September 2006:
Vol. 313. no. 5795, p. 1849
DOI: 10.1126/science.313.5795.1849h
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Significant insights into the mechanism of protein translation have come from recent high-resolution structures of the 50S and 30S ribosomal subunits. Progress has also been made on determining the structure of the whole ribosome, but a high-resolution view of the entire ribosome bound to its ligands has been lacking. Selmer et al. (p. 1935, published online 7 September) have determined the structure of the Thermus thermophilis ribosome complexed with messenger RNA (mRNA) and transfer RNA (tRNA) at 2.8 angstrom resolution. The structure reveals details of the interaction of the mRNA and tRNA ligands with the ribosome and the role of proteins and metal ions in the formation of inter-subunit bridges.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)