1OIZ
The Molecular Basis of Vitamin E Retention: Structure of Human Alpha-Tocopherol Transfer Protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-09-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.144, 113.775, 67.433 |
Unit cell angles | 90.00, 98.95, 90.00 |
Refinement procedure
Resolution | 30.000 - 1.880 |
R-factor | 0.197 |
Rwork | 0.195 |
R-free | 0.22600 |
Structure solution method | OTHER |
RMSD bond length | 0.010 |
RMSD bond angle | 1.300 * |
Data reduction software | XDS |
Data scaling software | XDS |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.900 |
High resolution limit [Å] | 1.880 | 1.880 |
Rmerge | 0.051 | 0.443 |
Total number of observations | 345927 * | |
Number of reflections | 54206 | |
<I/σ(I)> | 20.2 | 3.2 |
Completeness [%] | 99.3 | 93.1 |
Redundancy | 6.4 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 | 18 * | 5% PEG 6000, 0.1 M HEPES PH 7.5, 15% (V/V) MPD |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 18 (mg/ml) | |
2 | 1 | reservoir | PEG6000 | 5 (%(w/v)) | |
3 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
4 | 1 | reservoir | MPD | 15 (%(v/v)) |