1US4

PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-04-15
Detector	RIGAKU IMAGE PLATE
Wavelength(s)	0.9, 0.9789, 0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	51.518, 68.092, 81.381
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.000 * - 1.750
R-factor	0.178
Rwork	0.178
R-free	0.20600
Structure solution method	MAD
RMSD bond length	0.005
RMSD bond angle	22.600 *
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	CNS
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.810
High resolution limit [Å]	1.750	1.750
Rmerge	0.067	0.153
Total number of observations	123941 *
Number of reflections	28082
<I/σ(I)>	25.1	13.6
Completeness [%]	95.2	98
Redundancy	4.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5	291	VAPOUR DIFFUSION METHOD, 10 MG/ML OF PROTEIN SOLUTION WAS MIXED WITH RESERVOIR SOLUTION (20.3% PEG4000, 0.09M SODIUM CITRATE PH 5.0) AND EQUILIBRATED AGAINST RESERVOIR SOLUTION AT ROOM TEMPERATURE (291 K). CRYSTALS IN FORM OF PARALLELEPIPEDS WERE GROWN TO 0.05X0.05X0.15 MM WITHIN 10 DAYS. CRYOPROTECTANT CONTENT: 25% PEG4000, 18% ETHYLENE GLYCOL AND 0.1M SODIUM CITRATE PH 5.0.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG4000	20.3 (%)
3	1	reservoir	sodium citrate	0.09 (M)	pH5.