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1OIZ

The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein

Experimental procedure
Experimental methodSINGLE WAVELENGTH
Source typeSYNCHROTRON
Source detailsSLS BEAMLINE X06SA
Synchrotron siteSLS
BeamlineX06SA
Temperature [K]100
Detector technologyCCD
Collection date2002-09-15
DetectorMARRESEARCH
Spacegroup nameP 1 21 1
Unit cell lengths45.144, 113.775, 67.433
Unit cell angles90.00, 98.95, 90.00
Refinement procedure
Resolution30.000 - 1.880
R-factor0.197
Rwork0.195
R-free0.22600
Structure solution methodOTHER
RMSD bond length0.010
RMSD bond angle1.300

*

Data reduction softwareXDS
Data scaling softwareXDS
Refinement softwareREFMAC (5.1.24)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]30.0001.900
High resolution limit [Å]1.8801.880
Rmerge0.0510.443
Total number of observations345927

*

Number of reflections54206
<I/σ(I)>20.23.2
Completeness [%]99.393.1
Redundancy6.43.6
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, sitting drop

*

7.518

*

5% PEG 6000, 0.1 M HEPES PH 7.5, 15% (V/V) MPD
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein18 (mg/ml)
21reservoirPEG60005 (%(w/v))
31reservoirHEPES0.1 (M)pH7.5
41reservoirMPD15 (%(v/v))

219140

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