4F4E

Crystal structure of Aromatic-amino-acid aminotransferase from Burkholderia pseudomallei covalently bound to pyridoxal phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2012-05-09
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 21 21 2
Unit cell lengths	134.920, 74.820, 85.280
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.1625
Rwork	0.161
R-free	0.19640
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4eff
RMSD bond length	0.014
RMSD bond angle	1.586
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.060	0.017	0.465
Number of reflections	80481	1021	5781
<I/σ(I)>	20.33	81.55	2.47
Completeness [%]	99.7	98	98.7
Redundancy	5	6.4	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Emerald Bio JCSG+ screen C1: 20% PEG8000, 100 mM phosphate/citrate, pH 4.2, 200 mM sodium chloride, 36.1 mg/mL BupsE.01471.a.A1 PW 34948 + 2.5 mM PLP, tray 233390c1, cryoprotectant: 10/20% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 290K