4OO0

Crystal Structure of Maf-like protein BceJ2315_23540 from Burkholderia cenocepacia

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-07-31
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 61 2 2
Unit cell lengths	84.200, 84.200, 260.060
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.150
R-factor	0.1791
Rwork	0.177
R-free	0.22120
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ex2
RMSD bond length	0.009
RMSD bond angle	1.739
Data scaling software	XSCALE
Phasing software	PHASER (2.5.5)
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.210
High resolution limit [Å]	2.150	9.620	2.150
Rmerge	0.060	0.025	0.545
Number of reflections	30677	428	2207
<I/σ(I)>	25.61	58.03	4.2
Completeness [%]	99.6	91.8	99.6
Redundancy	9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	289	JCSG+(a6): 20% PEG-1000, 100mM Sodium phosphate dibasic/ citric acid, pH=4.2, 200mM Lithium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 289K