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The three-dimensional structure of yeast tRNA Asp, an elongator tRNA with a short variable loop, has been solved to high resolution in two non-isomorphous but closely related orthorhombic crystal forms. A first attempt to solve the structure by molecular replacement using the molecular structure of yeast tRNA Phe as a model was unsuccessful although the tRNA molecule could be correctly oriented within 10 ° by the rotation function. The phase problem was solved by the MIR approach. Two heavy-atom derivatives (Gd and Au) were used as markers. A 3.5 resolution map could thus be interpreted and a Kendrew skeletal model built. The folding of the molecule * Present address: Immunologic Structurale, Institut Pasteur, 28 rue du Dr Roux, 75015 Paris, France. 5" To whom reprint requests should be addressed. 0108-7681/86/030272-09501.50 is similar to that originally found for yeast tRNA P~e. Major differences concern the relative positioning of the acceptor and anticodon stems: the more open conformation confers to the tRNA Asp molecule a boomerang-like shape. Crystal packing involves selfcomplementary GUC anticodon interactions through a crystallographic twofold axis. This is the first visualization of such an interaction at the molecular level.

Three-dimensional structure of yeast tRNA Asp . I. Structure determination