1OIZ

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


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.55% PEG 6000, 0.1 M HEPES PH 7.5, 15% (V/V) MPD
Crystal Properties
Matthews coefficientSolvent content
2.6954.28

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 45.144α = 90
b = 113.775β = 98.95
c = 67.433γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDMARRESEARCH2002-09-15MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONSLS BEAMLINE X06SASLSX06SA

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Merge I (Observed)Net I Over Average Sigma (I)RedundancyNumber Reflections (All)Number Reflections (Observed)Observed Criterion Sigma (F)Observed Criterion Sigma (I)B (Isotropic) From Wilson Plot
11.883099.30.05120.26.454206
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R Merge I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
11.881.993.10.4433.23.6

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONOTHERTHROUGHOUT1.883051495271199.40.1970.1950.226RANDOM25.73
Temperature Factor Modeling
Anisotropic B[1][1]Anisotropic B[1][2]Anisotropic B[1][3]Anisotropic B[2][2]Anisotropic B[2][3]Anisotropic B[3][3]
-1.64-1.21-0.952.21
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg5.605
r_scangle_it2.621
r_scbond_it1.598
r_angle_refined_deg1.281
r_mcangle_it1.002
r_mcbond_it0.534
r_nbd_refined0.219
r_symmetry_vdw_refined0.186
r_symmetry_hbond_refined0.125
r_xyhbond_nbd_refined0.121
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_1_deg5.605
r_scangle_it2.621
r_scbond_it1.598
r_angle_refined_deg1.281
r_mcangle_it1.002
r_mcbond_it0.534
r_nbd_refined0.219
r_symmetry_vdw_refined0.186
r_symmetry_hbond_refined0.125
r_xyhbond_nbd_refined0.121
r_chiral_restr0.084
r_bond_refined_d0.01
r_gen_planes_refined0.004
r_bond_other_d
r_angle_other_deg
r_dihedral_angle_2_deg
r_dihedral_angle_3_deg
r_dihedral_angle_4_deg
r_gen_planes_other
r_nbd_other
r_nbtor_refined
r_nbtor_other
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_other
r_mcangle_other
r_scbond_other
r_scangle_other
r_long_range_B_refined
r_long_range_B_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms4289
Nucleic Acid Atoms
Solvent Atoms294
Heterogen Atoms150

Software

Software
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling