3K9W

Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-dephospho Coenzyme A

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	IMAGE PLATE
Collection date	2009-09-18
Detector	MAR scanner 300 mm plate
Wavelength(s)	0.97953
Spacegroup name	I 4 3 2
Unit cell lengths	134.431, 134.431, 134.431
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	26.360 - 1.600
R-factor	0.192
Rwork	0.191
R-free	0.20690
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3IKZ
RMSD bond length	0.008
RMSD bond angle	1.193
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.067	0.555
Number of reflections	27383
<I/σ(I)>	32.8	3.98
Completeness [%]	99.0	100
Redundancy	10.7	9.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.6	289	CSHT condition F1: 0.2 M ammonium sulfate, 0.1 M NaOAc pH 4.6, 30% PEG MME 2000, 20% EG as cryo-protectant, 19.2 mg/mL protein in 25 mM Hepes pH 7.0, 0.3 M NaCl, 10% glycerol, 5 mM DTT, crystal tracking ID 204963f1, VAPOR DIFFUSION, SITTING DROP, temperature 289K