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The crystal structure of yeast phenylalanine tRNA at 1.93 Å resolution: A classic structure revisited

Published online by Cambridge University Press:  01 August 2000

HUIJING SHI
Affiliation:
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA
PETER B. MOORE
Affiliation:
Department of Chemistry, Yale University, New Haven, Connecticut 06520-8107, USA
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Abstract

The crystal structure of the monoclinic form of yeast phenylalanine tRNA has been redetermined at a resolution of 1.93 Å. The structure of yeast tRNAphe described here is more accurate than its predecessors not only because it incorporates higher resolution data, but also because it has been refined using techniques that had not been developed when its predecessors were determined more than 20 years ago. The 1.93 Å resolution version of this structure differs interestingly from its predecessors in its details. In loop regions particularly, the backbone torsion angles in the new structure are not the same as those reported earlier. Several new divalent cation binding sites have been identified, and the water structure that has emerged is also different.

Type
Research Article
Copyright
© 2000 RNA Society

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