1LN2

Crystal Structure of Human Phosphatidylcholine Transfer Protein in Complex with Dilinoleoylphosphatidylcholine (Seleno-Met Protein)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9A
Synchrotron site	NSLS
Beamline	X9A
Temperature [K]	117
Detector technology	CCD
Collection date	2001-04-20
Detector	MARRESEARCH
Wavelength(s)	0.979
Spacegroup name	P 4 21 2
Unit cell lengths	134.700, 134.700, 82.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	67.350 - 2.900
R-factor	0.234
Rwork	0.231
R-free	0.29300
Structure solution method	MAD
RMSD bond length	0.019
RMSD bond angle	24.800 *
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	67.400	3.080
High resolution limit [Å]	2.900	2.900
Rmerge	0.048	0.128 *
Total number of observations	164647 *
Number of reflections	32130 *
Completeness [%]	99.7 *	99.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.7	298	sodium formate, sodium acetate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	sodium formate	3.4-3.8 (M)
2	1	reservoir	sodium acetate	0.1 (M)	pH5.7
3	1	reservoir	dithiothreitol	5 (mM)