4IYQ

Crystal structure of divalent ion tolerance protein CutA1 from Ehrlichia chaffeensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-05-12
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.977408
Spacegroup name	P 1 21 1
Unit cell lengths	87.490, 32.580, 89.080
Unit cell angles	90.00, 119.65, 90.00

Refinement procedure

Resolution	19.355 - 2.550
R-factor	0.171
Rwork	0.168
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1uku
RMSD bond length	0.008
RMSD bond angle	1.044
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.1)
Refinement software	PHENIX (dev_1269)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	20.000	2.620
High resolution limit [Å]	2.550	11.400	2.550
Rmerge	0.114	0.034	0.489
Number of reflections	14664	148	1055
<I/σ(I)>	10.77	29.8	2.76
Completeness [%]	99.1	73.6	99.4
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	EB Synergy screen c10: 40% iso-propanol, 15% PEG 8000, 100mM imidazole/HCl, EhchA.00496.a.A1.PB00060 at 21mg/ml, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K