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. |