3QAT

Crystal structure of acyl-carrier-protein-S-malonyltransferase from Bartonella henselae

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	2010-12-21
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97946
Spacegroup name	P 21 21 21
Unit cell lengths	50.190, 98.010, 138.180
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.600
R-factor	0.1597
Rwork	0.159
R-free	0.18230
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ezo
RMSD bond length	0.013
RMSD bond angle	1.374
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.640
High resolution limit [Å]	1.600	7.160	1.600
Rmerge	0.070	0.024	0.460
Number of reflections	89635	1147	5790
<I/σ(I)>	20.24	53.3	3.5
Completeness [%]	98.8	99.3	87.4
Redundancy	8.1		5.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	BaheA.00141.a.A1 PS00852 at 21.8 mg/mL against JCSG+ screen condition A5, 0.2 M magnesium formate, 20% PEG 3350 with 25% EG as cryo-protectant, crystal tracking ID 218778a5, VAPOR DIFFUSION, SITTING DROP, temperature 289K