3BE1

Dual specific bH1 Fab in complex with the extracellular domain of HER2/ErbB-2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-07-13
Detector	ADSC QUANTUM 315
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	62.324, 115.056, 208.171
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 - 2.900
R-factor	0.222
Rwork	0.236
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3bdy
RMSD bond length	0.009
RMSD bond angle	1.210
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	3.000
High resolution limit [Å]	2.900	2.900
Number of reflections	34149
<I/σ(I)>	18.5
Completeness [%]	100.0	100
Redundancy	5.7	5.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	292	Crystals of the Fab/HER2 complex were obtained by mixing protein solution (11 mg/ml protein, 25 mM Tris-HCl pH 8 and 150 mM sodium chloride) with crystallization buffer containing 25% w/v PEG2000, 0.1M MES pH 6.5. Before data collection the crystals were flash frozen in liquid nitrogen with 20% Ethylene Glycol as cryo-protectant, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K