6VEL

Crystal Structure of Human E-cadherin bound by mouse monoclonal antibody 66E8Fab

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	2019-07-18
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 31 2 1
Unit cell lengths	142.170, 142.170, 90.320
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.540 - 2.650
R-factor	0.1961
Rwork	0.194
R-free	0.23580
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2o72
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.18.2-3874)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.540	46.540	2.720
High resolution limit [Å]	2.650	11.850	2.650
Rmerge	0.061	0.023	0.595
Rmeas	0.065	0.025	0.631
Total number of observations	269932
Number of reflections	30906	383	2243
<I/σ(I)>	24.68	54.39	3.56
Completeness [%]	99.9	96	100
Redundancy	8.734	7.154	8.984
CC(1/2)	0.999	0.999	0.920

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	A complex of HosaA.19747.a.KW2, MumuA.20194.a.LG23, and MumuA.20195.a.LH23 was crystallized at 10.4 mg/ml at 14C and mixed 1:1 with 12.5% (w/v) PEG 4000, 20% (v/v) 1,2,6-hexanetriol, 0.1M GlyGly/AMPD pH 8.5, 0.03M of each Lithium sulfate, Sodium sulfate, and Potassium sulfate. Tray 307437a10: puck ckt8-9.