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

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

doi:10.1016/j.dib.2016.03.003

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 entericasubsp. 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 s 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).

Highlights

Data ArticleFluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str
Analyzed High concentration protein stocks were diluted in the Fluorescence-based thermal shift (FTS) analysis buffer
The latter three molecules were identified as the StAcrR binders employing a fluorescence polarization experimental approach

Summary

Data Article

Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. 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. B.A. Manjasetty et al / Data in Brief 7 (2016) 537–539 against various pathological conditions of sixteen small-molecule ligands that increase thermal stability of StAcrR.

Specifications Table

Value of the data