4ZND

2.55 Angstrom resolution structure of 3-phosphoshikimate 1-carboxyvinyltransferase (AroA) from Coxiella burnetii in complex with shikimate-3-phosphate, phosphate, and potassium

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2011-10-06
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97850
Spacegroup name	P 61 2 2
Unit cell lengths	94.795, 94.795, 233.668
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.990 - 2.550
R-factor	0.16892
Rwork	0.166
R-free	0.23801
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3slh
RMSD bond length	0.020
RMSD bond angle	2.007
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0107)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.590
High resolution limit [Å]	2.550	2.550
Rmerge	0.089	0.538
Number of reflections	21004
<I/σ(I)>	16.8	3.6
Completeness [%]	99.2	100
Redundancy	6.3	6.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	Protein solution: 7.5 mg/ml, 0.25 M NaCl, 0.01 M Tris-HCl pH 8.3 Crystallization condition: Classics II F8 (Qiagen): 0.2 M Ammonium sulfate, 0.1 m Hepes pH 7.5, 25% (w/v) PEG 3350