4QKU

Crystal structure of a putative hydrolase 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	2014-04-03
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	73.640, 110.550, 116.160
Unit cell angles	90.00, 106.61, 90.00

Refinement procedure

Resolution	50.000 - 2.450
R-factor	0.21
Rwork	0.208
R-free	0.24920
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.316
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.6)
Refinement software	REFMAC (5.8.0071)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.510
High resolution limit [Å]	2.450	10.960	2.450
Rmerge	0.146	0.041	0.555
Number of reflections	65019	745	4765
<I/σ(I)>	10.06	25.83	3.14
Completeness [%]	99.1	96	99
Redundancy	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4	289	BuceA.00077.a.B1.PW37289 at 20.8 mg/mL against JCSG+ screen condition B1, 0.1 M Na citrate pH 4.0, 0.8 M ammonium sulfate cryo-protected with 20% ethylene glycol, crystal tracking ID 246960b1, unique puck ID rhw0-1, VAPOR DIFFUSION, SITTING DROP