1KJY

Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RUH3R
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-07-17
Detector	RIGAKU RAXIS IV++
Wavelength(s)	1.5418
Spacegroup name	P 2 2 21
Unit cell lengths	69.510, 82.040, 187.240
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.700
R-factor	0.238 *
Rwork	0.238
R-free	0.29900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1bof
RMSD bond length	0.007
RMSD bond angle	1.370 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.111	0.480
Total number of observations	136468 *
Number of reflections	29900 *	2875 *
<I/σ(I)>	14	3.4
Completeness [%]	99.1	97.5
Redundancy	4.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5 *	18 *	Cesium Sulfate, sodium acetate, glycerol, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	17 (mg/ml)	and 1.5-fold molar excess R14GL peptide
2	1	drop	Tris	10 (mM)	pH7.5
3	1	drop		1 (mM)
4	1	drop	GDP	0.010 (mM)
5	1	drop	glycerol	5 (%)
6	1	reservoir	sodium acetate	100 (mM)	pH4.6
7	1	reservoir	glycerol	10 (%)
8	1	reservoir	caesium sulphate	1.4 (M)