9EVN

Plasmodium falciparum apical membrane antigen FVO

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-2
Synchrotron site	ESRF
Beamline	ID23-2
Temperature [K]	100
Detector technology	CCD
Collection date	2012-05-01
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.8726
Spacegroup name	P 21 21 21
Unit cell lengths	38.276, 94.216, 96.202
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.110 - 2.000
R-factor	0.17889
Rwork	0.177
R-free	0.21890
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.009
RMSD bond angle	1.467
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0415)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.110	2.050
High resolution limit [Å]	2.000	2.000
Number of reflections	24245	1754
<I/σ(I)>	8.1
Completeness [%]	99.8
Redundancy	3.6
CC(1/2)	0.994	0.491

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		290	Crystals of PfAMA1-FVO were obtained by mixing 1 micro-L of protein and 1 micro-L of reservoir buffer containing 35 % PEG 5000 monomethylether, 0.1M Tris pH 8.5 and 0.2M Li2SO4. The final protein concentration was 3.5 mg/ml. Cryo-protecting buffer for PfAMA1-FVO crystals consisted of the crystallisation buffer with 15% of glycerol (v/v).