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))