5VIU

Crystal Structure of Acetylornithine Aminotransferase from Elizabethkingia anophelis

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	2017-03-22
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	136.600, 77.470, 104.960
Unit cell angles	90.00, 129.46, 90.00

Refinement procedure

Resolution	42.354 - 1.650
R-factor	0.1558
Rwork	0.155
R-free	0.18010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2oat
RMSD bond length	0.006
RMSD bond angle	0.806
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	42.354	42.354	1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.037	0.018	0.514
Rmeas	0.043	0.022	0.601
Total number of observations	384308
Number of reflections	101355	1176	7472
<I/σ(I)>	20.68	59.5	2.52
Completeness [%]	99.4	96.1	99.5
Redundancy	3.792	3.51	3.761
CC(1/2)	0.999	0.999	0.862

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	ElanA.01026.a.B1.PW37983 at 19.6 mg/ml, incubated with 3 mM ornithine and alpha-ketoglutaric acid and mixed 1:1 with an equal volume JCSG+(a3): 20% (w/v) PEG-3350, 200 mM ammonium citrate dibasic, cryoprotected with 20% ethylene glycol