5TDN
Crystal structure of the Fab fragment of anti-HER2 antibody 4D5 with redesigned heavy and light chain interfaces
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-15 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.98 |
Spacegroup name | P 1 |
Unit cell lengths | 38.761, 79.597, 85.983 |
Unit cell angles | 113.58, 93.06, 102.30 |
Refinement procedure
Resolution | 23.506 - 1.630 |
R-factor | 0.1869 |
Rwork | 0.185 |
R-free | 0.21530 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fve |
RMSD bond length | 0.007 |
RMSD bond angle | 1.087 |
Data reduction software | iMOSFLM (0.2.8) |
Data scaling software | Aimless (0.2.8) |
Phasing software | PHENIX (1.9_1692) |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.506 | 1.720 |
High resolution limit [Å] | 1.630 | 1.630 |
Rmerge | 0.036 | 0.400 |
Rmeas | 0.051 | |
Rpim | 0.036 | |
Total number of observations | 212578 | |
Number of reflections | 108557 | |
<I/σ(I)> | 13.4 | |
Completeness [%] | 95.6 | 93.9 |
Redundancy | 2 | 2 |
CC(1/2) | 0.996 | 0.717 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 292 | 20% PEG3,350, 0.04 M Citrate, 0.06 M BTP, pH6.4 |