Tong, L A <br/><br/>
Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP.  [electronic resource] 

 -  Journal of molecular biology  Feb 1991 
 - 503-16 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1016/0022-2836(91)90753-s  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Cloning, Molecular<br/>Computer Simulation<br/>Crystallography<br/>GTP-Binding Proteins--ultrastructure<br/>Glycine--chemistry<br/>Guanosine Triphosphate--metabolism<br/>Hydrogen Bonding<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutation<br/>Oncogene Protein p21(ras)--ultrastructure<br/>Protein Conformation<br/>Proto-Oncogene Proteins p21(ras)--ultrastructure<br/>Recombinant Proteins--ultrastructure<br/>Salts<br/>Solubility<br/>Structure-Activity Relationship<br/>Valine--chemistry<br/>X-Ray Diffraction