9FXK

Transcription repressor NrdR from E. coli, AMPPNP/ATP-bound state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-02-25
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97963
Spacegroup name	P 21 21 21
Unit cell lengths	84.797, 129.791, 143.877
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	96.370 - 2.331
R-factor	0.2259
Rwork	0.224
R-free	0.25650
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.860
Data reduction software	autoPROC
Data scaling software	XDS
Phasing software	PHASER
Refinement software	BUSTER (2.11.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	96.372	2.569
High resolution limit [Å]	2.331	2.331
Rmerge	0.204	2.451
Rmeas	0.212	2.547
Rpim	0.057	0.687
Number of reflections	51826	2591
<I/σ(I)>	10	1.5
Completeness [%]	75.7	15.1
Redundancy	13.7	13.6
CC(1/2)	0.996	0.427

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein at 8 mg/ml in 1.5 mM ADP, 1.1 mM AMPPNP, 25 mM Tris-HCl pH 9 (at 277 K), 300 mM NaCl, 1 mM TCEP, 10 mM MgCl2. 150 nL protein were mixed with with 50 nL reservoir solution containing 0.1 M Bis-Tris propane pH 7.5, 0.2 M potassium thiocyanate, 20% (w/v) PEG3350 at 293 K. Crystals were harvested in paraffin oil.