4TM5

X-ray crystal structure of a D-amino acid aminotransferase from Burkholderia thailandensis E264 bound to the co-factor pyridoxal phosphate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	CCD
Collection date	2014-04-29
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.12709
Spacegroup name	C 2 2 21
Unit cell lengths	61.830, 70.020, 140.010
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.347 - 1.603
R-factor	0.1557
Rwork	0.154
R-free	0.19010
RMSD bond length	0.009
RMSD bond angle	1.288
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((phenix.refine: 1.9_1692))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.640
High resolution limit [Å]	1.600	7.170	1.600
Rmerge	0.047	0.018	0.402
Rmeas	0.051	0.020	0.462
Total number of observations	234322
Number of reflections	40085	507	2720
<I/σ(I)>	25.61	69.03	3.24
Completeness [%]	99.4	95.7	93.4
Redundancy	5.84		3.86

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	400 nl of protein + 400 nl of Morpheus condition C4 - 0.1 M MES/imidazole pH 6.5, 12.5% PEG1000, 12.5% PEG3350, 12.5% MPD, 30 mM sodium nitrate, 30 mM disodium hydrogen phosphate, 30 mM ammonium sulfate