2OZP

Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from Thermus thermophilus

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B2
Synchrotron site	SPring-8
Beamline	BL26B2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-14
Detector	ADSC QUANTUM 210
Wavelength(s)	0.97882, 0.97935, 0.90000
Spacegroup name	P 62 2 2
Unit cell lengths	144.957, 144.957, 85.128
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.010
R-factor	0.185
Rwork	0.185
R-free	0.20700
Structure solution method	MAD
RMSD bond length	0.007
RMSD bond angle	1.541
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE (2.10)
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	126.000	2.080
High resolution limit [Å]	2.010	2.010
Rmerge	0.091	0.489
Number of reflections	64827
<I/σ(I)>	13.3	7.9
Completeness [%]	100.0	100
Redundancy	21.3	22

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	80mM Sodium Hepes, 1.6% PEG 400, 1.6M Ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	80mM Sodium Hepes, 1.6% PEG 400, 1.6M Ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	80mM Sodium Hepes, 1.6% PEG 400, 1.6M Ammonium sulfate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K