4JWP

Crystal structure of Ribosomal-protein-alanine N-acetyltransferase from Brucella melitensis in complex with Acetyl CoA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU MICROMAX-007 HF
Temperature [K]	100
Detector technology	CCD
Collection date	2012-02-15
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	C 1 2 1
Unit cell lengths	72.420, 74.380, 67.550
Unit cell angles	90.00, 91.62, 90.00

Refinement procedure

Resolution	41.580 - 2.000
R-factor	0.1754
Rwork	0.173
R-free	0.22480
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	native structure pdb entry 4J3G
RMSD bond length	0.013
RMSD bond angle	1.444
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.5.2)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.069	0.027	0.301
Number of reflections	24170	282	1348
<I/σ(I)>	27.17	79.05	5.74
Completeness [%]	99.5	99	95.4
Redundancy	10.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Microlytics MCSG1, C7: 200mM CaCl2, 100mM Tris pH 8.5, 25% PEG 4000G 3350, BrabA.17352.a.A1.PS01094 at 20mg/ml, 2.5mM CoA, VAPOR DIFFUSION, SITTING DROP, temperature 290K