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A MODEL OF PROTEIN-SYNTHESIS BASED ON CRYOELECTRON MICROSCOPY OF THE E-COLI RIBOSOME
Author(s): FRANK J, ZHU J, PENCZEK P, LI YH, SRIVASTAVA S, VERSCHOOR A, RADERMACHER M, GRASSUCCI R, LATA RK, AGRAWAL RK
Source: NATURE    Volume: 376    Issue: 6539    Pages: 441-444    Published: AUG 3 1995  
Times Cited: 283     References: 24     
Abstract: THE ribosome is formed by assembly of proteins and nucleic acids, and synthesizes proteins according to genetic instructions in all organisms. Many of the biochemical steps of this fundamental process are known, but a detailed understanding requires a well-defined structural model of the ribosome. Electron microscopy combined with image reconstruction of two-dimensional crystals or single ribosomes(4) has been the most promising technique, but the resolution of the resulting models has been insufficient. Here we report a 25-Angstrom reconstruction of the ribosome from Escherichia coli, obtained by combining 4,300 projections of ice-embedded single particles. Our new reconstruction reveals a channel in the small ribosomal subunit and a bifurcating tunnel in the large subunit which may constitute pathways for the incoming message and the nascent polypeptide chain, respectively. Based on these new findings, a three-dimensional model of the basic framework of protein synthesis is presented.
Document Type: Article
Language: English
Reprint Address: FRANK, J (reprint author), NEW YORK STATE DEPT HLTH, WADSWORTH CTR LABS & RES, BOX 509, ALBANY, NY 12201 USA
Addresses:
1. SUNY ALBANY, DEPT BIOMED SCI, ALBANY, NY 12222 USA
2. SUNY ALBANY, DEPT COMP SCI, ALBANY, NY 12222 USA
Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF
Subject Category: Multidisciplinary Sciences
IDS Number: RM639
ISSN: 0028-0836
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