5TSA

Crystal structure of the Zrt-/Irt-like protein from Bordetella bronchiseptica with bound Zn2+

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	193
Detector technology	PIXEL
Collection date	2016-10-21
Detector	DECTRIS PILATUS3 S 6M
Wavelength(s)	1.2782
Spacegroup name	I 1 2 1
Unit cell lengths	55.006, 61.073, 94.394
Unit cell angles	90.00, 104.02, 90.00

Refinement procedure

Resolution	33.373 - 2.400
R-factor	0.2143
Rwork	0.212
R-free	0.25710
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	TBA
RMSD bond length	0.008
RMSD bond angle	0.965
Data scaling software	Aimless (0.5.28)
Phasing software	PHASER (2.6.0)
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	33.373	41.910	2.490
High resolution limit [Å]	2.400	8.960	2.400
Rmerge	0.116	0.055	0.829
Rmeas	0.125
Rpim	0.048
Total number of observations	80183
Number of reflections	11734
<I/σ(I)>	11.7
Completeness [%]	97.5	97.6	93.6
Redundancy	6.8	6.2	7
CC(1/2)	0.998	0.998	0.819

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	LIPIDIC CUBIC PHASE	7.5	294	protein concentration: 15 mg/mL; buffer: 10 mM Hepes pH 7.3, 300 mM NaCl, 5% Glycerol, 0.02% DDM; crystallization condition: 0.1 M Sodium chloride, 0.1 M Cadmium chloride hemi, 0.1 M Tris-HCl pH 7.5, 33% PEG 400