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Wiley, FEBS Letters, 2-3(552), p. 207-213

DOI: 10.1016/s0014-5793(03)00926-8

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High-throughput screening of structural proteomics targets using NMR

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

We applied a high-throughput strategy for the screening of targets for structural proteomics of Xanthomonas axonopodis pv citri. This strategy is based on the rapid (1)H-(15)N HSQC NMR analysis of bacterial lysates containing selectively (15)N-labelled heterologous proteins. Our analysis permitted us to classify the 19 soluble candidates in terms of 'foldedness', that is, the extent to which they present a well-folded solution structure, as reflected by the quality of their NMR spectra. This classification allowed us to define a priority list to be used as a guide to select protein candidates for further structural studies.