6CXY

Crystal Structure of Human E-cadherin bound by mouse monoclonal antibody Fab mAb-1_19A11

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2018-03-22
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	122.680, 77.470, 110.940
Unit cell angles	90.00, 92.91, 90.00

Refinement procedure

Resolution	40.091 - 2.200
R-factor	0.1644
Rwork	0.163
R-free	0.19700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2o72 4web
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.8.2)
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.091	40.091	2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.082	0.025	0.587
Rmeas	0.094	0.029	0.672
Total number of observations	221388
Number of reflections	52838	627	3868
<I/σ(I)>	13.4	36.44	2.6
Completeness [%]	99.9	98	99.9
Redundancy	4.19	3.836	4.246
CC(1/2)	0.997	0.999	0.784

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	HosaA.19747.a.KW2.PC00156 at 10.3 mg/ml in a buffer containing 50 mM Tris, pH = 8, 150 mM NaCl, and 3 mM CaCl2 was mixed 0.1 uL + 0.1 uL with Wizard 3/4 (h12): 15% (w/v) PEG-20,000, 0.1 M HEPES/ NaOH, pH = 7.0. The crystal was cryoprotected with 20% ethylene glycol. Tray: 299140h12, puck: qxp2-3