1N8Z

Crystal structure of extracellular domain of human HER2 complexed with Herceptin Fab

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X4A
Synchrotron site	NSLS
Beamline	X4A
Temperature [K]	110
Detector technology	CCD
Detector	ADSC QUANTUM 4
Spacegroup name	P 21 21 21
Unit cell lengths	66.170, 109.770, 175.140
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	30.000 * - 2.520
R-factor	0.22521
Rwork	0.222
R-free	0.28600 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB 1M6B
RMSD bond length	0.016
RMSD bond angle	1.790 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.19)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	2.580
High resolution limit [Å]	2.500	2.520
Rmerge	0.068 *	0.510 *
Total number of observations	164522 *
Number of reflections	42223
Completeness [%]	96.4	82.4 *
Redundancy	3.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	298	20-30% PEG 5000 MME, 0.1M MES pH6.5, 0.2M ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
2	1	drop	Tris	10 (mM)	pH7.5
3	1	reservoir	PEG4000	15-30 (%)
4	1	reservoir	sodium citrate	50 (mM)	pH5.4
5	1	reservoir	EDTA	10 (mM)