1S8G

Crystal structure of Lys49-Phospholipase A2 from Agkistrodon contortrix laticinctus, fatty acid bound form

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LNLS BEAMLINE D03B-MX1
Synchrotron site	LNLS
Beamline	D03B-MX1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-10-11
Detector	MAR scanner 345 mm plate
Wavelength(s)	1.544
Spacegroup name	P 41 21 2
Unit cell lengths	81.897, 81.897, 49.902
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	57.300 - 2.300
R-factor	0.20663
Rwork	0.205
R-free	0.24700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ppa
RMSD bond length	0.005
RMSD bond angle	0.929
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	MOLREP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	57.300	2.410
High resolution limit [Å]	2.300	2.300
Rmerge	0.118	0.382 *
Total number of observations	101833 *
Number of reflections	7960
<I/σ(I)>		1.7
Completeness [%]	98.1	99.7
Redundancy	6.2	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	291	cacodylate, ammonium sulfate, PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	30 (%(w/v))
2	1	reservoir	sodium cacodylate	0.1 (M)	pH6.5
3	1	reservoir	ammonium sulfate	0.2 (M)
4	1	drop	protein	10 (mg/ml)