Journal:

Article Title: On the Evolution of Structure in Aminoacyl-tRNA Synthetases

doi: 10.1128/MMBR.67.4.550-573.2003

Figure Lengend Snippet: Full structural dendrogram of the class I aminoacyl-tRNA synthetase catalytic domains. Crystal structures with high sequence identity, i.e., ∼100%, have been omitted (see Computational Methods). The ordering according to the QR transformation and the SCOP domain codes is listed on the right. Also listed are the crystallographic resolution and the identity of cocrystallized substrates. Yellow bars indicate the noise in the crystallographic data arising either from variations in resolution or from conformation between the structures crystallized with and without substrates. In terms of QH, regions of reliability for sequence- and structure-based phylogenetic analysis are indicated on the graph, and there is a considerable region of overlap between the two methods. Faded lines indicate decreasing reliability of phylogenetic interpretations. (Trees were drawn with MATLAB version 6.5 [Mathworks, Inc.].)

Article Snippet: Faded lines indicate decreasing reliability of phylogenetic interpretations. (Trees were drawn with MATLAB version 6.5 [Mathworks, Inc.].) fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window FIG. 10. caption a7 Full structural dendrogram of the class II synthetases.

Techniques: Sequencing, Transformation Assay