@article{de60042f0600463d9d312a5bca3f264a,
title = "1H, 13C, and 15N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase",
abstract = "The interaction between DnaG primase and DnaB helicase is essential for stimulating primer synthesis during bacterial DNA replication. The interaction occurs between the N-terminal domain of helicase and the C-terminal domain of primase. Here we present the 1H, 13C, and 15N backbone and side-chain resonance assignments for the C-terminal helicase interaction domain of Staphylococcus aureus primase.",
keywords = "DnaG, Helicase, NMR, Primase, Resonance assignments, Staphylococcus aureus",
author = "Shortridge, {Matthew D.} and Griep, {Mark A.} and Robert Powers",
note = "Funding Information: Acknowledgments This work was supported in part by a grant from the UNL/UNMC Collaborative Research Fund to M.G. and grants from National Institute of Allergy and Infectious Diseases (R21AI081154), Nebraska Tobacco Settlement Biomedical Research Development Funds, Nebraska EPSCoR, the Maude Hammond Fling Faculty Research Fellowship, and a Nebraska Research Council Interdisciplinary Research Grant to R.P. The research was performed in facilities renovated with support from the NIH (RR015468-01). The authors would like to thank the Rocky Mountain Regional 900 MHz NMR Facility for contributing NMR data to this project.",
year = "2012",
month = apr,
doi = "10.1007/s12104-011-9320-7",
language = "English (US)",
volume = "6",
pages = "35--38",
journal = "Biomolecular NMR Assignments",
issn = "1874-2718",
publisher = "Springer Netherlands",
number = "1",
}