2XTZ

Crystal structure of the G alpha protein AtGPA1 from Arabidopsis thaliana

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2009-11-16
Detector	MARRESEARCH MX300
Spacegroup name	P 21 21 21
Unit cell lengths	67.130, 119.347, 161.725
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	96.030 - 2.340
R-factor	0.21247
Rwork	0.211
R-free	0.25378
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1fqj
RMSD bond length	0.011
RMSD bond angle	1.249
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.5.0109)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	44.600	2.360
High resolution limit [Å]	2.340	2.340
Rmerge	0.110	0.840
Number of reflections	55808
<I/σ(I)>	17.5	1.9
Completeness [%]	100.0	100
Redundancy	6	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	277	CRYSTALS OF ATGPA1 WERE GROWN AT 4 DEGREES CELSIUS USING THE HANGING-DROP VAPOR-DIFFUSION METHOD. DROPS CONTAINED 1.5 UL OF PROTEIN SOLUTION (20 MG/ML ATGPA1 IN 25 MM TRIS-HCL, PH 7.4, 5% (V/V) GLYCEROL, 150 MM SODIUM CHLORIDE, 1 MM DTT, 500 UL GTP-GAMMA-S) AND WERE EQUILIBRATED AGAINST 1.5 UL OF 0.3 M MAGNESIUM SULFATE, 0.1 M SODIUM CACODYLATE, PH 6.0, 21% (W/V) PEG 8000. INITIALLY OBTAINED CRYSTALS WERE USED FOR MACROSEEDING. CRYSTALS REACHED THEIR FINAL ROD-SHAPE FORM WITHIN 14 DAYS AFTER MACROSEEDING AND WERE CRYOPROTECTED IN THE MOTHER LIQUOR WITH 8% (V/V) GLYCEROL.