title: The crystal structure of eEF1A refines the functional predictions of an evolutionary analysis of rate changes among elongation factors.
authors.forename: Eric A
authors.initials: EA
authors.lastname: Gaucher
authors.forename: Ujjwal K
authors.initials: UK
authors.lastname: Das
authors.forename: Michael M
authors.initials: MM
authors.lastname: Miyamoto
authors.forename: Steven A
authors.initials: SA
authors.lastname: Benner
mesh_terms: D001665:Binding Sites; D003461:Crystallography; D004926:Escherichia coli / Q000737:chemistry* / Q000235:genetics; D019143:Evolution, Molecular; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D020648:Peptide Elongation Factor 1 / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D020648:Peptide Elongation Factor 1; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu