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1AS0

GTP-GAMMA-S BOUND G42V GIA1

Experimental procedure
Source typeSYNCHROTRON
Source detailsCHESS BEAMLINE A1
Synchrotron siteCHESS
BeamlineA1
Temperature [K]110
Detector technologyCCD
Collection date1996-01
Spacegroup nameP 32 2 1
Unit cell lengths78.950, 78.950, 105.290
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution8.000 - 2.000
R-factor0.206
Rwork0.206
R-free0.25900
Structure solution methodDIFFERENCE FOURIER
Starting model (for MR)1gia
RMSD bond length0.010
RMSD bond angle22.800

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Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
Low resolution limit [Å]15.000
High resolution limit [Å]2.000
Rmerge0.104
Number of reflections19678
<I/σ(I)>10.4
Completeness [%]75.0
Redundancy2.3
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1VAPOR DIFFUSION, HANGING DROP6

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20

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THE PROTEIN WAS CRYSTALLIZED IN HANGING DROPS USING 4M (NH4)2SO3 AS THE PRECIPITANT. 50 MM HEPES, PH 8.0, 10 MM MGSO4, 10 MM DTT AND 0.2 MM GTP-GAMMA-S WAS THE BUFFER., vapor diffusion - hanging drop
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein7.5-10 (mg/ml)
21drop0.75-1.0 (M)
31dropsodium acetate50 (mM)
41reservoir1.5-2.0 (M)
51reservoirsodium acetate100 (mM)

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