1KXJ

The Crystal Structure of Glutamine Amidotransferase from Thermotoga maritima

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2001-10-01
Detector	SBC-2
Wavelength(s)	0.97916, 0.97938
Spacegroup name	P 32 2 1
Unit cell lengths	82.045, 82.045, 176.352
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.000 * - 2.800
R-factor	0.229
Rwork	0.229
R-free	0.27400
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.800
Data reduction software	HKL-2000
Data scaling software	d*TREK
Phasing software	SnB
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.900
High resolution limit [Å]	2.800	2.800
Rmerge	0.106	0.377
Number of reflections	32696
<I/σ(I)>	12	2.2
Completeness [%]	99.9	99.3
Redundancy	3.7	3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	21 *	2 M mono-Ammonium dihydrogen Phosphate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	mono-ammonium dihydrogen phosphate	2.0 (M)
2	1	reservoir	Tris-HCl	100 (mM)	pH8.5