8REL

Fab of an anti-PvAMA1 monoclonal antibody

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2006-12-04
Detector	ADSC QUANTUM 210r
Wavelength(s)	0.9340
Spacegroup name	P 1 21 1
Unit cell lengths	53.490, 61.520, 116.990
Unit cell angles	90.00, 97.49, 90.00

Refinement procedure

Resolution	42.240 - 2.100
R-factor	0.20206
Rwork	0.200
R-free	0.25461
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.013
RMSD bond angle	1.065
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.8.0415)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.020	2.210
High resolution limit [Å]	2.100	2.100
Rmerge	0.139	0.608
Rmeas	0.162	0.713
Rpim	0.083	0.369
Number of reflections	41875	4784
<I/σ(I)>	7.7	2.1
Completeness [%]	94.8	74.7
Redundancy	3.8	3.6
CC(1/2)	0.991	0.503

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		290	Crystals of Fab8.1.1 were obtained by mixing 1 micro-L of protein and 1 micro-L of reservoir containing 24% PEG 4000, 80 mM sodium acetate pH 4.6 and 0.16 M ammonium acetate. The final protein concentration was 3.6 mg/ml. Cryo-protecting buffer for FabF8.1.1 consisted of the crystallisation buffer where PEG was increased to 30% added with 15% of glycerol (v/v).