In his News Focus "Tapping DNA for structures produces a trickle" (1 Nov., p. 948), Robert Service presents an informative viewpoint about the progress of the structural genomics consortia. He describes how a number of consortia have targeted a vast number of proteins but only solved a small fraction of them. Although this is true, it is important to realize that structural genomics projects have been organized to evaluate large numbers of candidate targets, often of the same protein in different organisms, and simultaneously work on them in parallel. The aim is to determine the structure of representatives of particular protein families; thus, the representatives that do not come to fruition are not necessarily failures but are often simply the consequence of success elsewhere. For example, according to the International Structural Genomics Target Tracking Database (1), over 360 new three-dimensional protein structures have been completed by the various consortia and many more are nearly done. These proteins, which were selected because of their unique position in sequence space, have actually shed light on further thousands of homologous proteins whose structures can now be modeled for the first time. Thus, the output of structural genomics is highly leveraged, being much greater than the absolute number of new experimental structures.
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Gerstein et al. (2003) studied this question.