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

Babu A. Manjasetty; Andrei S. Halavaty; Chi Hao Luan; Jerzy Osipiuk; Rory Mulligan; Keehwan Kwon; Wayne F. Anderson; Andrzej Joachimiak

doi:10.1016/j.dib.2016.03.003

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

Babu A. Manjasetty, Andrei S. Halavaty^*, Chi Hao Luan, Jerzy Osipiuk, Rory Mulligan, Keehwan Kwon, Wayne F. Anderson, Andrzej Joachimiak

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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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 (δT_m), 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)
Pages (from-to)	537-539
Number of pages	3
Journal	Data in Brief
Volume	7
DOIs	https://doi.org/10.1016/j.dib.2016.03.003
State	Published - Jun 1 2016

Keywords

AcrR
Fluorescence-based thermal shift analysis
High-throughout screening
Infectious diseases
Salmonella enterica
TetR
Transcriptional regulator

ASJC Scopus subject areas

General

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.dib.2016.03.003

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@article{eb3d938258384386a12d78d22990c4d2,

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) (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).",

keywords = "AcrR, Fluorescence-based thermal shift analysis, High-throughout screening, Infectious diseases, Salmonella enterica, TetR, Transcriptional regulator",

author = "Manjasetty, {Babu A.} and Halavaty, {Andrei S.} and Luan, {Chi Hao} and Jerzy Osipiuk and Rory Mulligan and Keehwan Kwon and Anderson, {Wayne F.} and Andrzej Joachimiak",

note = "Funding Information: 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 . Publisher Copyright: {\textcopyright} 2016.",

year = "2016",

month = jun,

day = "1",

doi = "10.1016/j.dib.2016.03.003",

language = "English (US)",

volume = "7",

pages = "537--539",

journal = "Data in Brief",

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T1 - Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2

AU - Manjasetty, Babu A.

AU - Halavaty, Andrei S.

AU - Luan, Chi Hao

AU - Osipiuk, Jerzy

AU - Mulligan, Rory

AU - Kwon, Keehwan

AU - Anderson, Wayne F.

AU - Joachimiak, Andrzej

N1 - Funding Information: 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 . Publisher Copyright: © 2016.

PY - 2016/6/1

Y1 - 2016/6/1

N2 - 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).

AB - 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).

KW - AcrR

KW - Fluorescence-based thermal shift analysis

KW - High-throughout screening

KW - Infectious diseases

KW - Salmonella enterica

KW - TetR

KW - Transcriptional regulator

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DO - 10.1016/j.dib.2016.03.003

M3 - Article

C2 - 27054155

AN - SCOPUS:84960408986

SN - 2352-3409

VL - 7

SP - 537

EP - 539

JO - Data in Brief

JF - Data in Brief

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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