Peter B. Moore

TL;DR: The crystal structure of the large ribosomal subunit from Haloarcula marismortui is determined at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins.

TL;DR: It is established that the ribosome is a ribozyme and the catalytic properties of its all-RNA active site are addressed and the mechanism of peptide bond synthesis appears to resemble the reverse of the acylation step in serine proteases.

TL;DR: A system for naming ribosomal proteins is described, designed so that new names are similar enough to old names to be easily recognized, but are written in a format that unambiguously identifies them as 'new system' names.

TL;DR: Comparing the structures and locations of the 50S ribosomal proteins from H.marismortui and D.radiodurans revealed striking examples of molecular mimicry, illustrating that identical RNA structures can be stabilized by unrelated proteins.

TL;DR: X-ray crystallographic electron density maps of the large ribosomal subunit from Haloarcula marismortui are generated at various resolutions up to 9 A using data from crystals that diffract to 3 A, demonstrating the correctness of the EM model and its placement in the unit cell.