3NZT

2.0 Angstrom Crystal structure of Glutamate--Cysteine Ligase (gshA) ftom Francisella tularensis in Complex with AMP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2010-03-08
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 65
Unit cell lengths	89.849, 89.849, 151.468
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.410 - 2.000
R-factor	0.16548
Rwork	0.164
R-free	0.19598
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2d32
RMSD bond length	0.012
RMSD bond angle	1.372
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0102)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.030
High resolution limit [Å]	2.000	2.000
Rmerge	0.063	0.468
Number of reflections	46618
<I/σ(I)>	25.2	3.9
Completeness [%]	100.0	100
Redundancy	5.7	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	295	protein: 7.3 mg/mL, 0.5M Sodium chloride, Tris-HCl (pH 8.3), 1mM AMPPNP, 1mM Magnesium chloride, screen: ClassicsII, drop A2, 0.1M Sodium acetate (pH 4.5), 2M Ammonium sulphate, Cryo: 1.8M Ammonium sulphate, 25% Sucrose, VAPOR DIFFUSION, SITTING DROP, temperature 295K