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Title: Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2

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) (http://dx.doi.org/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).

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
OSTI Identifier:
1324834
Alternate Identifier(s):
OSTI ID: 1629106
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Published Article
Journal Name:
Data in Brief
Additional Journal Information:
Journal Name: Data in Brief Journal Volume: 7 Journal Issue: C; Journal ID: ISSN 2352-3409
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Fluorescence-based thermal shift analysis; Infectious diseases; Transcriptional regulator; TetR; AcrR; Salmonella enterica; High-throughout screening

Citation Formats

Manjasetty, Babu A., Halavaty, Andrei S., Luan, Chi-Hao, Osipiuk, Jerzy, Mulligan, Rory, Kwon, Keehwan, Anderson, Wayne F., and Joachimiak, Andrzej. Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2. United States: N. p., 2016. Web. https://doi.org/10.1016/j.dib.2016.03.003.
Manjasetty, Babu A., Halavaty, Andrei S., Luan, Chi-Hao, Osipiuk, Jerzy, Mulligan, Rory, Kwon, Keehwan, Anderson, Wayne F., & Joachimiak, Andrzej. Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2. United States. https://doi.org/10.1016/j.dib.2016.03.003
Manjasetty, Babu A., Halavaty, Andrei S., Luan, Chi-Hao, Osipiuk, Jerzy, Mulligan, Rory, Kwon, Keehwan, Anderson, Wayne F., and Joachimiak, Andrzej. Wed . "Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2". United States. https://doi.org/10.1016/j.dib.2016.03.003.
@article{osti_1324834,
title = {Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2},
author = {Manjasetty, Babu A. and Halavaty, Andrei S. and Luan, Chi-Hao and Osipiuk, Jerzy and Mulligan, Rory and Kwon, Keehwan and Anderson, Wayne F. and Joachimiak, Andrzej},
abstractNote = {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) (http://dx.doi.org/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).},
doi = {10.1016/j.dib.2016.03.003},
journal = {Data in Brief},
number = C,
volume = 7,
place = {United States},
year = {2016},
month = {6}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1016/j.dib.2016.03.003

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