1FE5

SEQUENCE AND CRYSTAL STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM COMMON KRAIT (BUNGARUS CAERULEUS) AT 2.4 RESOLUTION: IDENTIFICATION AND CHARACTERIZATION OF ITS PHARMACOLOGICAL SITES.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1999-09-17
Detector	MARRESEARCH
Spacegroup name	R 3 2
Unit cell lengths	57.980, 57.980, 57.980
Unit cell angles	92.02, 92.02, 92.02

Refinement procedure

Resolution	9.990 - 2.400 *
R-factor	0.201
Rwork	0.201
R-free	0.27100
RMSD bond length	0.007
RMSD bond angle	1.100 *
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *	2.600
High resolution limit [Å]	2.400 *	2.400 *
Rmerge	0.092 *	0.174 *
Number of reflections	4629
<I/σ(I)>	7.2
Completeness [%]	93.0	92 *
Redundancy	17.3	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.5 *	8 *	Ammonium sulphate, CaCl2, Dioxane, Sodium cacodylate , pH 7.0, VAPOR DIFFUSION, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)
3	1	drop		1.4 (M)
4	1	drop		1 (mM)
5	1	reservoir		3.5 (M)