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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.
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