1OIP

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 41 21 2
Unit cell lengths	77.810, 77.810, 128.360
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 1.950
R-factor	0.192
Rwork	0.190
R-free	0.22700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.012
RMSD bond angle	1.300 *
Data reduction software	XDS
Data scaling software	XDS
Phasing software	CNS
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.980
High resolution limit [Å]	1.950	1.950
Rmerge	0.062	0.559
Total number of observations	317025 *
Number of reflections	29375
<I/σ(I)>	22.8	3.5
Completeness [%]	99.7	97.7
Redundancy	10.8	6.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	5.6	18 *	12% PEG 6000, 0.1 M NA-CITRATE PH 5.6, 0.1 M LISO4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	reservoir	PEG6000	12 (%(w/v))
3	1	reservoir	sodium citrate	0.1 (M)	pH5.6
4	1	reservoir		0.1 (M)