3ONW

Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2009-11-30
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.000
Spacegroup name	P 2 2 21
Unit cell lengths	70.392, 83.679, 190.148
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	95.070 - 2.380
R-factor	0.22953
Rwork	0.228
R-free	0.26539
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2OM2 chain A
RMSD bond length	0.009
RMSD bond angle	1.086
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]	28.880	2.400
High resolution limit [Å]	2.380	2.380
Rmerge	0.065	0.761
Number of reflections	45328
<I/σ(I)>	27.3	2.2
Completeness [%]	98.8	100
Redundancy	6	6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	291	Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.9 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K