Thermodynamics, cooperativity and stability of the tetracycline repressor (TetR) upon tetracycline binding.

Palm GJ, Buchholz I, Werten S, Girbardt B, Berndt L, Delcea M, Hinrichs W
Biochim Biophys Acta Proteins Proteom :140404 (2020 Feb 27)
PMID: 32114262
doi: 10.1016/j.bbapap.2020.140404 		Submitted to SASBDB: 2019 Apr 11
Published in SASBDB:

SASDFD5 – Tetracycline repressor (class D), TetR(D)

Tetracycline repressor (class D) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tetracycline repressor (class D) dimer, 47 kDa Escherichia coli protein
Buffer: 50 mM Tris/HCl 150 mM NaCl 10 mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
RgGuinier 2.6 nm
Dmax 7.7 nm
VolumePorod 85 nm3

SASDFE5 – Tetracycline repressor (class D), TetR(D), in complex with 5a,6-anhydrotetracycline (ATc)

Tetracycline repressor (class D)5a,6-anhydrotetracycline experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tetracycline repressor (class D) dimer, 47 kDa Escherichia coli protein
5a,6-anhydrotetracycline dimer, 1 kDa
Buffer: 50 mM Tris/HCl 150 mM NaCl 10 mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
RgGuinier 2.6 nm
Dmax 6.8 nm
VolumePorod 77 nm3