7LON

Ornithine Aminotransferase (OAT) cocrystallized with its inactivator - (1S,3S)-3-amino-4-(difluoromethylene)cyclohexene-1-carboxylic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-03-25
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	1.127
Spacegroup name	P 31 1 2
Unit cell lengths	192.024, 192.024, 57.058
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	49.050 - 1.950
R-factor	0.2452
Rwork	0.243
R-free	0.27840
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oat
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHENIX
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.050	1.977
High resolution limit [Å]	1.943	1.943
Rmerge	0.174	1.599
Rpim	0.092	0.925
Number of reflections	87426	4085
<I/σ(I)>	4.2
Completeness [%]	99.5	93
Redundancy	8.5	7
CC(1/2)	0.997	0.745

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	The freshly prepared enzyme was buffer exchanged into 50 mM Tricine pH 7.8 and concentrated to a protein concentration of 6 mg/mL. For each hanging drop, 2 ul of protein solution was mixed with equal volume of well solution and 0.5 ul of 10 mM compound. The crystals with the best morphology and size grew in a final condition containing 12% PEG 6000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.