7LNM

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2017-10-21
Detector	ADSC QUANTUM 210r
Wavelength(s)	0.9787
Spacegroup name	P 32
Unit cell lengths	115.720, 115.720, 188.021
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	36.480 - 2.000
R-factor	0.159
Rwork	0.158
R-free	0.18600
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]	68.560	68.560	2.030
High resolution limit [Å]	2.000	10.950	2.000
Rmerge	0.118	0.070	1.086
Rmeas	0.136	0.082	1.284
Rpim	0.068	0.042	0.678
Total number of observations	749788	4224	33035
Number of reflections	190270	1136	9377
<I/σ(I)>	4.6	7.6	1.3
Completeness [%]	100.0	97.1	100
Redundancy	3.9	3.7	3.5
CC(1/2)	0.993	0.987	0.376

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 8000, 200 mM NaCl, 10% glycerol, 50 mM Tricine pH 7.8.