4EFF

Crystal structure of aromatic-amino-acid aminotransferase from Burkholderia pseudomallei

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	2012-03-21
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97860
Spacegroup name	P 31 2 1
Unit cell lengths	66.190, 66.190, 156.860
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 1.850
R-factor	0.187
Rwork	0.185
R-free	0.21600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3fsl CHAIN A
RMSD bond length	0.013
RMSD bond angle	1.526
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.078	0.524
Number of reflections	34726
<I/σ(I)>	20.49	3.9
Completeness [%]	99.5	100
Redundancy	7.3	7.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Emerald Bio JCSG+ screen: 14.4% PEG8000, 160 mM calcium acetate, 20% glycerol, Bupse.01471.a.A1 PW 34948 at 36.1 mg/mL, pH 7.50, VAPOR DIFFUSION, SITTING DROP, temperature 290K