3TCV

Crystal structure of a GCN5-related N-acetyltransferase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-06-16
Detector	RAYONIX MX-300
Wavelength(s)	1.03322
Spacegroup name	C 1 2 1
Unit cell lengths	102.490, 66.860, 91.690
Unit cell angles	90.00, 107.51, 90.00

Refinement procedure

Resolution	50.000 - 1.750
R-factor	0.1626
Rwork	0.161
R-free	0.18950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3pzj
RMSD bond length	0.011
RMSD bond angle	1.388
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.067	0.022	0.453
Number of reflections	58008	650	3617
<I/σ(I)>	13.81	37.61	2.65
Completeness [%]	97.1	91.2	82.3
Redundancy	3.7		3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	BrabA.17403.a.A1 OS01078 at 28.7 mg/mL against JCSG+ condition A3 0.2 M ammonium citrate, 20% PEG 3350 with 25% ethylene glycol as cryo-protectant, crystal tracking ID 223197a3, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K