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3UMR

Crystal structure of the G202D mutant of human G-alpha-i1

Replaces:  2EBC
Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeROTATING ANODE
Source detailsRIGAKU RU200
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date2006-12-06
DetectorRIGAKU RAXIS IV
Wavelength(s)1.54
Spacegroup nameI 4
Unit cell lengths121.952, 121.952, 67.382
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution23.917 - 2.040
R-factor0.1719
Rwork0.170
R-free0.21000
Structure solution methodMOLECULAR REPLACEMENT
Starting model (for MR)1as3
RMSD bond length0.011
RMSD bond angle1.251
Data reduction softwareHKL-2000
Data scaling softwareHKL-2000
Phasing softwarePHASER
Refinement softwarePHENIX ((phenix.refine: dev_887))
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]23.9202.060
High resolution limit [Å]2.0402.040
Rmerge0.0500.738
Number of reflections30856
<I/σ(I)>45.32
Completeness [%]97.979
Redundancy6.33.1
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION6.5291Protein: 10-20 mg/mL in 50 mM HEPES, pH 8.0, 1 mM EDTA, 100 microM GDP, 5 mM DTT; well solution: 1.9M ammonium sulfite, 0.1M sodium acetate, pH 6.0, VAPOR DIFFUSION, temperature 291K

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