4J2W

Crystal Structure of kynurenine 3-monooxygenase (KMO-396Prot-Se)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	CCD
Collection date	2011-12-08
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9795
Spacegroup name	P 1 21 1
Unit cell lengths	59.130, 99.400, 85.360
Unit cell angles	90.00, 105.61, 90.00

Refinement procedure

Resolution	38.600 - 2.600
R-factor	0.2013
Rwork	0.198
R-free	0.25850
Structure solution method	SAD
RMSD bond length	0.009
RMSD bond angle	1.277
Data reduction software	XDS
Data scaling software	XDS
Phasing software	SOLVE
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	38.600	2.710
High resolution limit [Å]	2.600	2.600
Rmerge	0.093	0.755
Number of reflections	29704
<I/σ(I)>	12	2.1
Completeness [%]	99.3	98.4
Redundancy		3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	277	Initial crystals of Saccharomyces cerevisiae KMO KMO-396Prot-Se were obtained by mixing 200 nl of 14 mg/ml protein in 20 mM ammonium acetate, pH 7.0, 150 mM NaCl and 7 mM 2-mercaptoethanol (buffer A) with 200 nl of a reservoir solution containing 0.1 M sodium acetate, pH 5.5, and 35 % isopropanol. , VAPOR DIFFUSION, SITTING DROP, temperature 277K