7OVU

Crystal structure of Arabidopsis thaliana NAT9 in complex with AcCoA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID29
Synchrotron site	ESRF
Beamline	ID29
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-12-14
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.976251
Spacegroup name	C 1 2 1
Unit cell lengths	67.202, 48.895, 60.123
Unit cell angles	90.00, 102.75, 90.00

Refinement procedure

Resolution	39.190 - 1.450
R-factor	0.1502
Rwork	0.149
R-free	0.18090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3eo4
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	39.190	1.500
High resolution limit [Å]	1.450	1.450
Rmerge	0.072
Number of reflections	33777	3306
<I/σ(I)>	15.9	1.2
Completeness [%]	99.7
Redundancy	13.1
CC(1/2)	1.000	0.509

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		291	AtNAT9 was concentrated to 15 mg/ml and incubated with a threefold molar excess of AcCoA for 18 h on ice. Crystallization drops contained 200 nl protein solution and 200 nl precipitant solution (0.1 M HEPES (pH 7) and 20 % PEG6000) and crystals appeared after seven days. The crystals were cryo-protected with 20 % glycerol and flash-frozen in liquid nitrogen.