4X48

Crystal structure of GluR2 ligand-binding core

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2009-09-18
Detector	ADSC QUANTUM 315
Wavelength(s)	1.075
Spacegroup name	P 21 21 2
Unit cell lengths	114.759, 164.965, 47.363
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.670 - 1.890
R-factor	0.1747
Rwork	0.173
R-free	0.19720
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lz5
RMSD bond length	0.010
RMSD bond angle	1.030
Data scaling software	SCALA (3.3.9)
Phasing software	BUSTER-TNT
Refinement software	BUSTER-TNT

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	164.965	164.965	1.990
High resolution limit [Å]	1.886	5.960	1.890
Rmerge		0.052	0.392
Rmeas	0.088
Rpim	0.035	0.024	0.293
Total number of observations	372534	14487	16680
Number of reflections	69522
<I/σ(I)>	13.7	26.7	2
Completeness [%]	94.8	93.4	71.9
Redundancy	5.4	6.1	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	The protein solution contained 7 mg/ml GluR2-S1S2J, 10mM (S)-Glu, 10mM HEPES (pH 7.5), 20mM NaCl and 1mM EDTA. Compound was added to a final concentration of 150micromolar from a 30mM DMSO stock. To this solution, an equal amount of reservoir solution containing 10% PEG 8000, 0.1 M ZnAc and 0.1M NaAc, pH 5.5 was added, and 2microlitre drops of this mixture were allowed to equilibrate by vapor diffusion over a 1mL reservoir. Crystals appeared in the drops in 3-5 days.