4J3G

Crystal structure of Ribosomal-protein-alanine N-acetyltransferase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-09-19
Detector	RIGAKU SATURN 944+
Wavelength(s)	0.9774
Spacegroup name	P 1
Unit cell lengths	39.110, 57.000, 73.420
Unit cell angles	86.55, 88.15, 88.76

Refinement procedure

Resolution	46.320 - 1.750
R-factor	0.1727
Rwork	0.171
R-free	0.21190
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2j8m
RMSD bond length	0.014
RMSD bond angle	1.323
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.1)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.058	0.027	0.457
Number of reflections	62171	706	4563
<I/σ(I)>	16.27	46.02	2.81
Completeness [%]	97.4	99.2	96
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	Microlytics MCSG1, 200mM ammoinum sulfate, 100mM HEPES/NaOH pH 7.5, 25% PEG 3350, BrabA.17352.a.A1.PS01094 at 20mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 290K