2XNS

Crystal Structure Of Human G alpha i1 Bound To A Designed Helical Peptide Derived From The Goloco Motif Of RGS14

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	2010-04-10
Detector	MARRESEARCH
Spacegroup name	I 2 3
Unit cell lengths	265.261, 265.261, 265.261
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.990 - 3.410
R-factor	0.22335
Rwork	0.223
R-free	0.24434
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2om2
RMSD bond length	0.006
RMSD bond angle	1.091
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]	40.000	3.420
High resolution limit [Å]	3.410	3.410
Rmerge	0.120	1.000
Number of reflections	42418
<I/σ(I)>	22.1	2.2
Completeness [%]	100.0	100
Redundancy	11.1	11.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5		HEXAGONAL CRYSTALS WERE GROWN BY HANGING DROP VAPOR DIFFUSION USING 1 MICROLITER PREMIXED GALPHA I1 AND GOLOCO PEPTIDE (1:1.5 MOLAR RATIO) AT 12 MG/ML IN BUFFER (10 MM TRIS PH 7.5, 1 MM MAGNESIUM CHLORIDE, 10 MICROMOLAR GDP, 5 MM DTT) AND 1 MICROLITER CRYSTALLIZATION SOLUTION (800 MM AMMONIUM SULFATE, 200 MM K/NA TARTRATE, 100 MM SODIUM CITRATE PH 5.5).