Abstract
The crystal structure of yeast phenylalanine transfer RNA in the monoclinic form has been solved at 2.5Å resolution. The entire model was initially built into the 3.0Å map based on the multiple isomorphous replacement method, and later rebuilt through a series of cycles of 2Fo-Fc maps at 2.5Å resolution omitting oligonucleotide segments of 3-10 residues at a time. The improved model coordinates have been subjected to several rounds of difference synthesis refinement that have reduced the R value from 0.470 to 0.274.
