6W7X

Crystal structure of N-acetylornithine aminotransferase from Stenotrophomonas maltophilia K279a

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-03-12
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 31 2 1
Unit cell lengths	63.820, 63.820, 172.480
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.530 - 1.900
R-factor	0.1839
Rwork	0.182
R-free	0.21270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4jev
RMSD bond length	0.005
RMSD bond angle	0.759
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MR-Rosetta
Refinement software	PHENIX (1.17.1)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.064	0.048	0.647
Rmeas	0.068	0.053	0.714
Number of reflections	33007	430	2403
<I/σ(I)>	15.7	27.69	2.33
Completeness [%]	99.8	93.3	99.9
Redundancy	7.265	5.66	5.505
CC(1/2)	0.998	0.995	0.921

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	29.8 mg/mL StmaA.01026.b.B1.PW38742 against Molecular Dimensions Morpheus screen, condition a7 (10% w/V PEG4000, 20% V/V glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 100 mM MOPS/HEPES sodium, pH 7.5), direct cryoprotection, tray 313920a7, puck mnd6-1