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1LXD

CRYSTAL STRUCTURE OF THE RAS INTERACTING DOMAIN OF RALGDS, A GUANINE NUCLEOTIDE DISSOCIATION STIMULATOR OF RAL PROTEIN

Experimental procedure
Source typeSYNCHROTRON
Source detailsNSLS BEAMLINE X12B
Synchrotron siteNSLS
BeamlineX12B
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1996-11-10
DetectorMARRESEARCH
Spacegroup nameC 1 2 1
Unit cell lengths105.282, 30.714, 51.326
Unit cell angles90.00, 94.57, 90.00
Refinement procedure
Resolution6.000 - 2.400
R-factor0.212
Rwork0.212
R-free0.29800
Structure solution methodMAD
RMSD bond length0.014
RMSD bond angle2.500
Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareMADSYS
Refinement softwareX-PLOR (3.85)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]10.0002.480
High resolution limit [Å]2.4002.400
Rmerge0.090

*

Number of reflections6485
<I/σ(I)>16.75.92
Completeness [%]99.399.5
Redundancy44
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion

*

8.5PROTEIN WAS CRYSTALLIZED FROM 20% PEG 8000, 0.1 M TRIS PH 8.5, AND 0.2 M CALCIUM ACETATE.
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5 (mg/ml)
101reservoirPEG800020 (%)
21dropdithiothreitol0.5 (mM)
31dropPMSF0.5 (mM)
41dropEDTA0.5 (mM)
51dropcalcium acetate0.1 (M)
61dropTris-HCl0.05 (mM)
71dropPEG800010 (%)
81reservoircalcium acetate0.2 (M)
91reservoirTris-HCl0.1 (M)

222415

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