4NOZ

Crystal Structure of an Organic Hydroperoxide Resistance Protein from Burkholderia cenocepacia

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2013-10-16
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 4 21 2
Unit cell lengths	121.190, 121.190, 64.140
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	85.690 - 2.220
R-factor	0.1633
Rwork	0.162
R-free	0.19510
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1zb8
RMSD bond length	0.013
RMSD bond angle	1.481
Data scaling software	XSCALE
Phasing software	PHASER (2.5.5)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	99.611		2.280
High resolution limit [Å]	2.220	9.930	2.220
Rmerge	0.063	0.016	0.466
Number of reflections	24096	308	1753
<I/σ(I)>	32.67	102.18	5.7
Completeness [%]	99.6	91.1	100
Redundancy	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	MCSG1(d2): 0.2M NaCl, 0.1M Bis-Tris:HCl, pH=6.5, 25% PEG-3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K