The bacterial ribosome at atomic resolution.
X-ray crystallographic structures have just been published for the 30S ribosomal subunit of Thermus thermophilus at 3.4 A resolution and for the 50S subunit of Haloarcula marismortui at 2.4 A. These eagerly awaited structures will provide an enormous boost to research into the mechanisms involved in protein biosynthesis.
Brimacombe
R
R
Max-Planck-Institut für Molekulare Genetik Ihnestrasse 73 14195, Berlin, Germany. brimacombe@molgen.mpg.de
D019843:Archaeal Proteins / Q000737:chemistry; D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D010458:Peptidyl Transferases / Q000737:chemistry / Q000378:metabolism; D010802:Phylogeny; D014176:Protein Biosynthesis; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry / Q000648:ultrastructure; D012270:Ribosomes / Q000737:chemistry* / Q000648:ultrastructure
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D012261:Ribonucleoproteins; D012313:RNA; D010458:Peptidyl Transferases