1R5L

Crystal Structure of Human Alpha-Tocopherol Transfer Protein Bound to its Ligand

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-20
Detector	ADSC QUANTUM 4r
Wavelength(s)	0.9818
Spacegroup name	P 21 21 21
Unit cell lengths	40.096, 77.151, 85.397
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 1.500
R-factor	0.187
Rwork	0.187
R-free	0.21300
Structure solution method	MAD
RMSD bond length	0.015
RMSD bond angle	22.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.550
High resolution limit [Å]	1.500	1.500
Rmerge	0.074 *	0.213 *
Total number of observations	325760 *
Number of reflections	79802
<I/σ(I)>	24.5	8.4
Completeness [%]	97.4	89.2
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.1	20 *	PEG 4000, TRIS base, sodium chloride, pH 8.10, VAPOR DIFFUSION, HANGING DROP, temperature 293K
1	VAPOR DIFFUSION, HANGING DROP	8.1	20 *	PEG 4000, TRIS base, sodium chloride, pH 8.10, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PMSF	0.1 (mM)
2	1	drop	protein	5 (mg/ml)
3	1	reservoir	PEG4000	5 (%(w/v))
4	1	reservoir	Tris-HCl	100 (mM)	pH8.0-8.4