8RMO
Crystal structure of anti-FLAG M2 Fab fragment bound to FLAG-tag peptide epitope
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-10-10 |
Detector | DECTRIS EIGER2 X 9M |
Wavelength(s) | 0.6199 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 87.432, 134.621, 41.798 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 73.326 - 1.163 |
Rwork | 0.158 |
R-free | 0.18550 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.564 |
Data reduction software | autoPROC |
Data scaling software | STARANISO |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.326 | 1.245 |
High resolution limit [Å] | 1.163 | 1.163 |
Rmerge | 0.151 | 6.867 |
Rmeas | 0.153 | 7.008 |
Rpim | 0.026 | 1.388 |
Number of reflections | 123223 | 6161 |
<I/σ(I)> | 16.525 | 1.526 |
Completeness [%] | 95.7 | 71.98 |
Redundancy | 36.99 | |
CC(1/2) | 0.999 | 0.610 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1 M TRIS 8 pH, 20 %w/v PEG 6K, 0.2 M NH4Cl |