1LLW

Structural studies on the synchronization of catalytic centers in glutamate synthase: complex with 2-oxoglutarate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-06-21
Detector	MARRESEARCH
Wavelength(s)	0.9
Spacegroup name	P 43 21 2
Unit cell lengths	166.521, 166.521, 219.874
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.000 - 2.700
R-factor	0.23591
Rwork	0.234
R-free	0.29300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ea0
RMSD bond length	0.020
RMSD bond angle	2.200 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.1.06)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	62.000 *	2.850
High resolution limit [Å]	2.700	2.700
Rmerge	0.088	0.289 *
Total number of observations	947721 *
Number of reflections	83666
<I/σ(I)>	4.5	2.9
Completeness [%]	98.1	92.7 *
Redundancy	4	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7 *	4 *	PEG4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	16 (mg/ml)
2	1	drop	PIPES-KOH	25 (mM)	pH7.0
3	1	drop	EDTA	1 (mM)
4	1	drop	glycerol	10 (%)
5	1	reservoir	PEG4000	24-30 (%(w/v))
6	1	reservoir	Tris-HCl	100 (mM)	pH8.5
7	1	reservoir	sodium acetate	200 (mM)