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Bioincorporation of telluromehionine into proteins: A promising new approach for X-ray structure analysis of proteins
Citation key 005.1997.budisa
Author Budisa, N. and Karnbock, W. and Steinbacher, S. and Humm, A. and Prade, L. and Neuefeind, T. and Moroder, L. and Huber, R.
Pages 616-623
Year 1997
DOI 10.1006/jmbi.1997.1132
Journal J. Mol. Biol.
Volume 270
Number 4
Abstract A simple and efficient method for the specific and quantitative replacement of the naturally occurring amino acid methionine by its isosteric analogue telluromethionine in the expression of recombinant proteins has been developed. The method requires a controlable and competitive expression system like the bacteriophage T7 polymerase/promoter in a methionine-auxotrophic host. Using methionine-auxotrophic Escherichia coli strains, incorporation of telluromethionine at high yields has been achieved for human recombinant annexin V, human mitochondrial transamidase, Arabidopsis glutathione-S-transferase and the N-terminal domain of Salmonella tailspike adhesion protein as confirmed by amino acid, mass-spectrometric and X-ray analyses. Expressed and purified telluromethionine-proteins and native proteins were found to crystallise isomorphously. In terms of efficient bio-expression, isomorphism of crystals and relative abundance of methionine residues, the production of telluromethionine-proteins as heavy-atom derivatives offers a valid and general approach in X-ray analysis by the method of multiple isomorphous replacement.
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