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1TAD

GTPASE MECHANISM OF GPROTEINS FROM THE 1.7-ANGSTROM CRYSTAL STRUCTURE OF TRANSDUCIN ALPHA-GDP-ALF4-

Experimental procedure
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X25
Synchrotron siteNSLS
BeamlineX25
Detector technologyIMAGE PLATE
Collection date1993-02-11
DetectorFUJI
Wavelength(s)0.95
Spacegroup nameP 1 21 1
Unit cell lengths74.900, 108.200, 79.000
Unit cell angles90.00, 111.70, 90.00
Refinement procedure
Resolution8.000 - 1.700
R-factor0.209
Rwork0.209
R-free0.26600
RMSD bond length0.007
RMSD bond angle1.200
Data reduction softwareDENZO
Phasing softwareX-PLOR
Refinement softwareX-PLOR
Data quality characteristics
 OverallOuter shell
High resolution limit [Å]1.700

*

1.700

*

Rmerge0.103

*

0.186

*

Number of reflections11658412535

*

Completeness [%]88.076.7

*

Redundancy34.22

*

Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Batch method

*

6

*

4

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
111protein20 (mg/ml)
211PEG800020 (%(w/v))
311200 (mM)
411sodium cacodylate100 (mM)
511beta-mercaptoethanol0.2 (%(v/v))
6115 (mM)
7110.1 (M)
81130 (mM)
911glycerol40 (%(v/v))

224004

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