5DWN

Crystal structure of Phosphinothricin N-acetyltransferase from Brucella ovis in complex with AcetylCoA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2015-03-16
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	71.100, 77.380, 135.840
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.852 - 1.950
R-factor	0.1578
Rwork	0.156
R-free	0.19680
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	native structure
RMSD bond length	0.006
RMSD bond angle	0.806
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.10_2155)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.067	0.024	0.465
Rmeas	0.072	0.026	0.499
Total number of observations	409137
Number of reflections	55358	696	4044
<I/σ(I)>	22.42	60.16	4.46
Completeness [%]	99.9	97.9	100
Redundancy	7.4		7.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Microlytics screen MCSG1, b9: 200mM MgCl2, 20% PEG 3350; BrovA.17352.a.B1.PS02313 at 4mg/ml, supplemented with 5mM NAD; cryo: 20% EG with 5mM AcCoA; tray 262506 b9; puck jbj3-8