4WD2

Crystal structure of an aromatic amino acid aminotransferase from Burkholderia cenocepacia J2315

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2014-08-25
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 31 1 2
Unit cell lengths	59.220, 59.220, 200.270
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	45.647 - 1.950
R-factor	0.1183
Rwork	0.116
R-free	0.15140
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3tat
RMSD bond length	0.005
RMSD bond angle	0.893
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.7)
Refinement software	PHENIX ((phenix.refine: dev_1779))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.090	0.031	0.346
Rmeas	0.095	0.033	0.387
Total number of observations	292285
Number of reflections	29633	385	1986
<I/σ(I)>	22.52	61.61	4.72
Completeness [%]	99.1	98.2	90.9
Redundancy	9.86		4.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	Rigaku Reagents JCSG+ screen d1: 24% PEG 1500, 20% glycerol; BuceA.01471.a.B1.PS01824 at 20 mg/ml + 2.5mM pyridoxal phosphate; di rect cryo; tray 257500 d1, puck zba1-4