4FID

Crystal structure of a heterotrimeric G-Protein subunit from entamoeba histolytica, EHG-ALPHA-1

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-03-05
Detector	MAR scanner 300 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	56.671, 57.174, 231.289
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.900 - 2.620
R-factor	0.193
Rwork	0.189
R-free	0.25800
Structure solution method	SAD
RMSD bond length	0.008
RMSD bond angle	1.205
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX (AUTOSOL)
Refinement software	PHENIX ((PHENIX.REFINE: 1.6_289))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.900	2.620
High resolution limit [Å]	2.600	2.600
Rmerge		0.982
Number of reflections	43503
<I/σ(I)>		2.6
Completeness [%]	99.3	100
Redundancy		13.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		5.6	291	EHG-ALPHA-1 AT 15 MG/ML IN CRYSTALLIZATION BUFFER (50 MM HEPES PH 6.5, 150 MM NACL, 10 MM MGCL2, 10 MM NAF, 30 MICROM ALCL3, AND 50 MICROM GDP) WAS MIXED 1:1 AND EQUILIBRATED AGAINST CRYSTALLIZATION SOLUTION CONTAINING 1.5 M AMMONIUM SULFATE, 175 MM K/NA TARTRATE, AND 100 MM SODIUM CITRATE PH 5.6. 250 MM AMMONIUM ACETATE WAS ADDED TO THE WELL SOLUTION AFTER SETTING THE DROPS, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K