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Structural proteomics of an archaeon

TitleStructural proteomics of an archaeon
Publication TypeJournal Article
Year of Publication2000
AuthorsChristendat, D, Yee, A, Dharamsi, A, Kluger, Y, Savchenko, A, Cort, JR, Booth, V, Mackereth, CD, Saridakis, V, Ekiel, I, Kozlov, G, Maxwell, KL, Wu, N, McIntosh, LP, Gehring, K, Kennedy, MA, Davidson, AR, Pai, EF, Gerstein, M, Edwards, AM, Arrowsmith, CH
JournalNature Structural Biology
Date PublishedOct
Type of ArticleArticle
ISBN Number1072-8368

A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, similar to 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility. implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics

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