8OG0
Crystal structure of MJF14-6-4-2 Fab fragment in complex with epitope peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-02-10 |
Detector | DECTRIS EIGER2 XE 16M |
Wavelength(s) | 0.976254 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 37.484, 66.700, 167.167 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 83.580 - 1.712 |
R-factor | 0.19704 |
Rwork | 0.195 |
R-free | 0.23117 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.361 |
Data reduction software | autoPROC (v1.0.5) |
Data scaling software | autoPROC (v1.0.5) |
Phasing software | PHASER (v2.5.0) |
Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 83.580 | 1.902 |
High resolution limit [Å] | 1.712 | 1.712 |
Rmerge | 0.208 | 1.609 |
Number of reflections | 37216 | 1626 |
<I/σ(I)> | 8.5 | |
Completeness [%] | 94.3 | |
Redundancy | 13 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5 | 293 | Sitting droplets were set up by mixing 1 ul of Fab fragments, 0.5 ul of peptide (1 mg/ml in 20 mM tris-HCl) and 1 ul crystallization buffer (24% PEG 6000, 0.1M Na-citrate pH 5.0). |