Download MendeleyStructural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
Lesley, S.A., Kuhn, P., Godzik, A., Deacon, A.M., Mathews, I., Kreusch, A., Spraggon, G., Klock, H.E., McMullan, D., Shin, T., Vincent, J., Robb, A., Brinen, L.S., Miller, M.D., McPhillips, T.M., Miller, M.A., Scheibe, D., Canaves, J.M., Guda, C., Jaroszewski, L., Selby, T.L., Elsliger, M.-A., Wooley, J., Taylor, S.S., Hodgson, K.O., Wilson, I.A., Schultz, P.G., Stevens, R.C.(2002) Proc Natl Acad Sci U S A 99: 11664-11669
- PubMed: 12193646
- DOI: https://doi.org/10.1073/pnas.142413399
- Primary Citation of Related Structures:
1KQ3, 1KQ4 - PubMed Abstract:
Structural genomics is emerging as a principal approach to define protein structure-function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima. By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline.
Organizational Affiliation:
Joint Center for Structural Genomics, Genomics Institute of the Novartis Research Foundation, 10675 John Jay Hopkins Drive, San Diego, CA 92121, USA. [email protected]
