5EUN

The Crystal Structure of Human Kynurenine Aminotransferase II, PLP-bound form, at 1.83 A

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2015-09-22
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.9537
Spacegroup name	P 43 21 2
Unit cell lengths	102.455, 102.455, 86.236
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.462 - 1.825
R-factor	0.1745
Rwork	0.173
R-free	0.19900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.716
Data reduction software	XDS
Data scaling software	Aimless (0.3.11)
Phasing software	PHENIX ((1.10.1_2155: 2015))
Refinement software	PHENIX ((1.10.1_2155: 2015))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.860	1.890
High resolution limit [Å]	1.825	1.830
Rmerge	0.023	0.186
Number of reflections	40742
<I/σ(I)>	17.6	2.9
Completeness [%]	98.5	85.1
Redundancy	2	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	Protein (1 uL) at a concentration of 7 mg/mL were mixed with an equal volume of a reservoir solution containing 200 mM NaCl, 0.1M NaCitrate pH 5.6, 24% PEG4K and equilibrated against 1 mL of a reservoir solution at 293 K.