6F5V

Crystal structure of the prephenate aminotransferase from Arabidopsis thaliana

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	CCD
Collection date	2011-10-21
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97967
Spacegroup name	P 1
Unit cell lengths	58.470, 73.240, 103.320
Unit cell angles	92.49, 87.22, 111.05

Refinement procedure

Resolution	23.702 - 1.700
R-factor	0.1737
Rwork	0.172
R-free	0.20120
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.075
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX (1.7.3_928)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	23.702	1.740
High resolution limit [Å]	1.700	1.700
Number of reflections	168766	11501
<I/σ(I)>	16.57	2.75
Completeness [%]	96.0	88.2
Redundancy	6.14	3.73

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION		293	0.1 M Na citrate pH 4.0, 11 % PEG 4K