Crystal structure of yeast tRNAAsp

Abstract
Two independent, 3-dimensional structures of yeast tRNAAsp, mainly differing by the conformation of the D loop, were obtained from a multiple isomorphous replacement (MIR) X-ray analysis at 3.5-.ANG. resolution. The folding of the ribose-phosphate backbone was similar to that for tRNAPhe; major differences of the relative positioning of the acceptor and anticodon stems and conformation of the loops in the 2 molecules was observed. Crystal packing involved self-complementary GUC anticodon interactions.