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1GG2

G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND

Experimental procedure
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE A1
Synchrotron siteCHESS
BeamlineA1
Temperature [K]100
Detector technologyCCD
Collection date1996-01
Spacegroup nameP 43
Unit cell lengths83.776, 83.776, 130.938
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution15.000 - 2.400
R-factor0.205
Rwork0.205
R-free0.28900
Structure solution methodREFINEMENT WITH WILD-TYPE MODEL (SAME CELL)
RMSD bond length0.011
RMSD bond angle24.300

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]25.0002.490
High resolution limit [Å]2.4002.400
Rmerge0.0730.301
Number of reflections32774
<I/σ(I)>11.42.28
Completeness [%]93.091
Redundancy2.552.2
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

721

*

pH 7.0
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG800018 (%)
21reservoirNa-HEPES100 (mM)pH7.0
31reservoirsodium acetate100 (mM)pH6.4
41reservoirn-beta-octyl-glucoside0.05 (%)
51reservoir2-propanol2 (%)
61dropprotein7.5 (mg/ml)

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