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1GFI

STRUCTURES OF ACTIVE CONFORMATIONS OF GI ALPHA 1 AND THE MECHANISM OF GTP HYDROLYSIS

Experimental procedure
Temperature [K]100
Spacegroup nameP 32 2 1
Unit cell lengths80.500, 80.500, 106.550
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution8.000 - 2.200
R-factor0.214
Rwork0.214
R-free0.28400
RMSD bond length0.012

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RMSD bond angle1.500

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Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 Overall
Low resolution limit [Å]15.000

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High resolution limit [Å]2.200

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Rmerge0.053

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Total number of observations96580

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Number of reflections19715
Completeness [%]97.8
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

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6

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21

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Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein25-30 (mg/ml)
21drop0.03 (M)
31drop5 (mM)
41drop5 (mM)
51dropdithiothreitol10 (mM)
61dropsodium acetate200 (mM)
71reservoirammonium sulfate1.8-1.9 (M)

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PDB entries from 2024-07-17

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