4AOA

Biochemical properties and crystal structure of a novel beta- phenylalanine aminotransferase from Variovorax paradoxus

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2010-07-27
Detector	ADSC QUANTUM 315r
Spacegroup name	P 21 21 21
Unit cell lengths	88.670, 99.880, 104.790
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	72.300 - 2.280
R-factor	0.18422
Rwork	0.182
R-free	0.22476
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CBF3 HOLO ENZYME STRUCTURE
RMSD bond length	0.008
RMSD bond angle	1.105
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	66.310	2.400
High resolution limit [Å]	2.280	2.280
Rmerge	0.100	0.160
Number of reflections	43283
<I/σ(I)>	10.9	7.5
Completeness [%]	99.8	99.8
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1