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1J78

Crystallographic analysis of the human vitamin D binding protein

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsEMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron siteEMBL/DESY, Hamburg
BeamlineX11
Temperature [K]100
Detector technologyIMAGE PLATE
Collection date1999-04-17
DetectorMARRESEARCH
Wavelength(s)0.9116
Spacegroup nameP 43
Unit cell lengths132.248, 132.248, 73.179
Unit cell angles90.00, 90.00, 90.00
Refinement procedure
Resolution29.380 - 2.310
R-factor0.2201

*

Rwork0.220
R-free0.25180

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Structure solution methodCOMBINED MAD AND MIRAS
RMSD bond length0.006
RMSD bond angle1.170

*

Data reduction softwareDENZO
Data scaling softwareSCALEPACK
Phasing softwareSHARP
Refinement softwareCNS (1.0)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0002.350
High resolution limit [Å]2.3102.310
Rmerge0.0310.209
Total number of observations187531

*

Number of reflections55444
<I/σ(I)>22.75.2
Completeness [%]99.299.6
Redundancy3.43.4
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.6293Verboven, C.C., (1995) J. Steroid Biochem. Mol. Biol., 54, 11.

*

Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11reservoirPEG4007.5 (%(v/v))
21reservoiracetate0.1 (M)pH4.6
31dropprotein30 (mg/ml)

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