Abstract
The fluorescence-based thermal shift (FTS) data presented here include Table S1 and Fig. S1, and are supplemental to our original research article describing detailed structural, FTS, and fluorescence polarization analyses of the Salmonella enterica subsp. entrica serovar Typhimurium str. LT2 multidrug transcriptional regulator AcrR (StAcrR) (doi:10.1016/j.jsb.2016.01.008) (Manjasetty et al., 2015 [1]). Table S1 contains chemical formulas, a Chemical Abstracts Service (CAS) Registry Number (CAS no.), FTS rank (a ligand with the highest rank) has the largest difference in the melting temperature (δTm), and uses as drug molecules against various pathological conditions of sixteen small-molecule ligands that increase thermal stability of StAcrR. Thermal stability of human enolase 1, a negative control protein, was not affected in the presence of various concentrations of the top six StAcrR binders (Fig. S1).
Original language | English (US) |
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Pages (from-to) | 537-539 |
Number of pages | 3 |
Journal | Data in Brief |
Volume | 7 |
DOIs | |
State | Published - Jun 1 2016 |
Funding
The CSGID project has been funded in whole or in part with Federal funds from the National Institute of Allergy and Infectious Diseases , National Institutes of Health , Department of Health and Human Services , under Contracts nos. HHSN272200700058C and HHSN272201200026C . We thank Sankar Krishnna for the human enolase 1 sample. The authors wish to thank members of the Structural Biology Center (SBC) at Argonne National Laboratory for their help with X-ray diffraction data collection. The operation of SBC beamlines is supported by the U.S. Department of Energy, Office of Biological and Environmental Research under Contract DE-AC02-06CH11357 .
Keywords
- AcrR
- Fluorescence-based thermal shift analysis
- High-throughout screening
- Infectious diseases
- Salmonella enterica
- TetR
- Transcriptional regulator
ASJC Scopus subject areas
- General