3V1L

Crystal Structure of the S112A/H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	CCD
Collection date	2009-11-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.033
Spacegroup name	I 41 2 2
Unit cell lengths	117.458, 117.458, 87.791
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	83.060 - 2.110
R-factor	0.1809
Rwork	0.179
R-free	0.21880
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.261
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	83.060	50.000	2.190
High resolution limit [Å]	2.110	4.540	2.110
Rmerge	0.126	0.059	0.367
Number of reflections	17692
<I/σ(I)>	7
Completeness [%]	97.8	100	80.6
Redundancy	7.6	9.9	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSING, SITTING DROP, MICROSEEDING	6.8	298	2.4 M Sodium malonate, pH 6.8, VAPOR DIFFUSING, SITTING DROP, MICROSEEDING, temperature 298K