7LK0

Ornithine Aminotransferase (OAT) cocrystallized with its potent inhibitor - (S)-3-amino-4,4-difluorocyclopent-1-enecarboxylic acid (SS-1-148)

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	2019-10-26
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	1.1271
Spacegroup name	P 31 1 2
Unit cell lengths	192.707, 192.707, 56.804
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	48.180 - 1.960
R-factor	0.248
Rwork	0.247
R-free	0.26750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1oat
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHASER
Refinement software	PHENIX (1.17.1_3660)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.180	1.989
High resolution limit [Å]	1.955	1.955
Rmerge	0.169	0.817
Rpim	0.083	0.604
Number of reflections	79187	3113
<I/σ(I)>	5.6	1.1
Completeness [%]	91.6	72.1
Redundancy	8.7	4.1
CC(1/2)	0.997	0.783

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	OAT was buffer exchanged into crystallization buffer (50 mM Tricine pH 7.8) supplied with 1 mM 2-ketoglutarate. Then the protein was concentrated to 6 mg/mL. For each hanging drop, 2 uL of protein solution was mixed with an equal volume of well solution and 0.5 uL of 10 mM SS-1-148. The crystals with the best morphology and size grew in a final condition containing 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8.