1KPM

First Structural Evidence of a Specific Inhibition of Phospholipase A2 by Vitamin E and its Implications in Inflammation: Crystal Structure of the Complex Formed between Phospholipase A2 and Vitamin E at 1.8 A Resolution.

Replaces:  1FE7

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	180
Detector technology	IMAGE PLATE
Collection date	1999-06-20
Detector	MARRESEARCH
Wavelength(s)	0.98
Spacegroup name	C 2 2 21
Unit cell lengths	75.790, 88.510, 78.040
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.197
Rwork	0.197
R-free	0.22800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cl5
RMSD bond length	0.014 *
RMSD bond angle	2.000 *
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.840
High resolution limit [Å]	1.800	1.800
Rmerge	0.038 *	0.084 *
Number of reflections	23652
<I/σ(I)>	9.93	2.1
Completeness [%]	96.0 *	99
Redundancy	6.6	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	6.5	298	20mM Sodium cacodylate, 1.4M Ammonium sulfate, 4mM Calcium chloride, 3% dioxane, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	drop	sodium cacodylate	20 (mM)	pH6.5
3	1	reservoir	ammonium sulfate	1.4 (M)
4	1	reservoir	dioxane	3 (%(v/v))