3U0E

Crystal structure of beta-ketoacyl synthase from Brucella melitensis in complex with fragment 9320

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	2009-09-15
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97740
Spacegroup name	C 1 2 1
Unit cell lengths	78.070, 83.750, 73.610
Unit cell angles	90.00, 121.50, 90.00

Refinement procedure

Resolution	20.000 - 1.600
R-factor	0.138
Rwork	0.137
R-free	0.15600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	native structure 3lrf
RMSD bond length	0.014
RMSD bond angle	1.589
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.640
High resolution limit [Å]	1.600	1.600
Rmerge	0.045	0.220
Number of reflections	53077
<I/σ(I)>	22.57	5.55
Completeness [%]	99.4	97.2
Redundancy	4.4	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	MD PACT SCREEN, H12: 20% PEG 3350, 100MM BISTRISPROPANE PH 8.5, 200MM NA-MALONATE, CRYSTAL SOAKED 100MM MES PH 6.5, 250MM NACL, 30% PEG 3350, 10% GLYCEROL, BrabA.00113.a.A1.PW25441 AT 22.9MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K