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Protein Science, Vol 5, Issue 1 174-177, Copyright © 1996 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Rapid screening for structural integrity of expressed proteins by heteronuclear NMR spectroscopy

A. M. GRONENBORN and G. M. CLORE
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520

A simple and rapid method based on (15)N labeling and (1)H-(15)N heteronuclear single quantum coherence spectroscopy is presented to directly assess the structural integrity of overexpressed proteins in crude Escherichia coli extracts without the need for any purification. The method is demonstrated using two different expression systems and two different proteins, the B1 immunoglobulin-binding domain of streptococcal protein G (56 residues) and human interleukin-1{beta} (153 residues). It is shown that high quality (1)H-(15)N correlation spectra, recorded in as little as 15 min and displaying only cross-peaks arising from the overexpressed protein of interest, can be obtained from crude E. coli extracts.
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