Abstract
We report the 1H, 13C and 15N backbone chemical shift assignments and secondary structure of the Escherichia coli protein BamC, a 32-kDa protein subunit that forms part of the BAM (Omp85) complex, the β-barrel assembly machinery present in all Gram-negative bacteria and which is essential for viability.
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Acknowledgments
We thank Christian Ludwig, Sara Whittaker and the other staff of The Henry Wellcome Building for Biomolecular NMR Spectroscopy, which is funded by the Wellcome Trust. This work was supported by the BBSRC and EU PRISM project [T.J.K and M.O.].
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Knowles, T.J., McClelland, D.M., Rajesh, S. et al. Secondary structure and 1H, 13C and 15N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli . Biomol NMR Assign 3, 203–206 (2009). https://doi.org/10.1007/s12104-009-9175-3
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DOI: https://doi.org/10.1007/s12104-009-9175-3