7LK1

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

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	2020-07-23
Detector	DECTRIS EIGER2 X 9M
Wavelength(s)	1.12713
Spacegroup name	P 32 2 1
Unit cell lengths	115.650, 115.650, 186.690
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	36.320 - 1.790
R-factor	0.2172
Rwork	0.216
R-free	0.24080
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	Inner shell	Outer shell
Low resolution limit [Å]	36.320	36.320	1.840
High resolution limit [Å]	1.790	8.010	1.790
Rmerge	0.084	0.035	2.487
Rpim	0.028	0.012	0.833
Number of reflections	136181	1687	9979
<I/σ(I)>	13.7	41.8	0.9
Completeness [%]	100.0	98.9	100
Redundancy	9.6	9	9.8
CC(1/2)	0.999	0.999	0.344

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	The holoenzyme crystals were first grown via a hanging drop vapor diffusion method. Each drop contained 2 uL of protein and 2 uL of well solution. The best crystallization condition contained 10% PEG 6000, 200 mM NaCl, 10% glycerol, 100 mM Tricine pH 7.8. Once the holoenzyme crystals reached their maximum size, 2 uL of 16 mM SS-1-148 was added to the drop with crystals. The crystals were soaked for 1 h, transferred into cryoprotective solution (well solution supplemented with 30% glycerol), and then flash-frozen in liquid nitrogen.