1US5

PUTATIVE GLUR0 LIGAND BINDING CORE WITH L-GLUTAMATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SPRING-8 BEAMLINE BL26B1
Synchrotron site	SPring-8
Beamline	BL26B1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2003-02-15
Detector	RIGAKU IMAGE PLATE RAXIS-V
Spacegroup name	P 21 21 21
Unit cell lengths	43.440, 69.476, 103.798
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.500
R-factor	0.184
Rwork	0.184
R-free	0.20500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1us4
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]	20.000 *	1.530
High resolution limit [Å]	1.500	1.500
Rmerge	0.065	0.362
Total number of observations	215880 *
Number of reflections	50003
<I/σ(I)>	20.7	3.1
Completeness [%]	97.7	94.7
Redundancy	4.32

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5	291	MICROBATCH METHOD UNDER OIL WAS USED. 20 MG/ML OF PROTEIN SOLUTION WAS MIXED WITH 22.5% PEG4000, 1M LITHIUM CHLORIDE AND 0.1M SODIUM CITRATE PH 5. THE CRYSTALLIZATION TEMPERATURE WAS 291 K. THE CRYSTALS IN FORM OF PARALLELEPIPEDS WERE GROWN TO 0.03X0.03X0.15 MM WITHIN ONE MONTH. CRYOPROTECTANT CONTAINED 25% PEG4000, 18% ETHYLENE GLYCOL, 1M LITHIUM CHLORIDE AND 0.1M SODIUM CITRATE PH 5.

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.