7STZ

Crystal Structure of Human E-cadherin EC1-5 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	2021-06-24
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9787
Spacegroup name	P 1 21 1
Unit cell lengths	85.340, 131.620, 201.760
Unit cell angles	90.00, 100.86, 90.00

Refinement procedure

Resolution	49.540 - 2.950
R-factor	0.1824
Rwork	0.182
R-free	0.20770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6cxy
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.20rc3-4406)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.540	49.540	3.030
High resolution limit [Å]	2.950	13.190	2.950
Rmerge	0.118	0.042	0.631
Rmeas	0.127	0.046	0.678
Total number of observations	685577
Number of reflections	92265	1050	6783
<I/σ(I)>	14.25	34.77	3.2
Completeness [%]	99.9	96.1	100
Redundancy	7.431	6.429	7.486
CC(1/2)	0.997	0.998	0.897

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	HosaA.19747.a.LS31.PC00180 at 11.5 mg/mL was mixed 2:1 (0.2 uL protein and 0.1 uL precipitant) with 0.1M sodium HEPES pH 7.0 and 15% w/v PEG4000 (ProPlex B11) and stored at 14C. The crystal was cryoprotected with 15% ethylene glycol. Tray: 321285b11, puck: ygq5-2.