1FB2

STRUCTURE OF PHOSPHOLIPASE A2 FROM DABOIA RUSSELLI PULCHELLA AT 1.95

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
Spacegroup name	C 2 2 21
Unit cell lengths	76.100, 88.050, 79.370
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.950
R-factor	0.216 *
Rwork	0.216
R-free	0.27200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cl5
RMSD bond length	0.006
RMSD bond angle	1.300
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	PROLSQ

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.020
High resolution limit [Å]	1.950	1.950
Rmerge	0.026 *	0.163 *
Number of reflections	17922 *
<I/σ(I)>	12.6	5.6
Completeness [%]	91.0 *	99 *
Redundancy	4.1	1.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	20mM Sodium Cacodylate, 1.4M Ammonium Sulphate, 4mM Calcium Chloride, 3% Dioxane, pH 6.5, 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 (%)