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1OMW

Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200H
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2002-06-15
DetectorMARRESEARCH
Wavelength(s)1.5418
Spacegroup nameC 1 2 1
Unit cell lengths188.200, 72.500, 122.790
Unit cell angles90.00, 115.20, 90.00
Refinement procedure
Resolution20.000 - 2.500
R-factor0.21648
Rwork0.202
R-free0.25196
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1ABG 1atp 1bak 1dk8
RMSD bond length0.024
RMSD bond angle2.035
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwareMOLREP
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0002.590
High resolution limit [Å]2.5002.500
Rmerge0.053

*

0.253

*

Number of reflections38258

*

<I/σ(I)>15.32.7
Completeness [%]73.612.7
Redundancy2.40.67
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP5.75277Lodowski, D.T., (2003) Acta Crystallogr., D59, 936.

*

1VAPOR DIFFUSION, HANGING DROP5.75277Lodowski, D.T., (2003) Acta Crystallogr., D59, 936.

*

1VAPOR DIFFUSION, HANGING DROP5.75277Lodowski, D.T., (2003) Acta Crystallogr., D59, 936.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein12 (mg/ml)
21reservoirMES100 (mM)pH5.25
31reservoir200 (mM)
41reservoirinositol-3,4,5-triphosphate1 (mM)
51reservoir5 (mM)
61reservoirPEG33506.9-7.8 (%)

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