2QHR
Crystal structure of the 13F6-1-2 Fab fragment bound to its Ebola virus glycoprotein peptide epitope.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-08-05 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.240, 70.300, 142.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.290 - 2.000 |
Rwork | 0.203 |
R-free | 0.24500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1yec |
RMSD bond length | 0.015 |
RMSD bond angle | 1.346 |
Data reduction software | d*TREK |
Data scaling software | d*TREK (9.4DDz) |
Phasing software | CNS |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.290 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.084 | 0.523 |
Number of reflections | 86917 | |
<I/σ(I)> | 6.8 | 1.7 |
Completeness [%] | 99.7 | 99.7 |
Redundancy | 4.02 | 3.51 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 295 | 16% (w/v) PEG 8000, 0.04M potassium phosphate, 20% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 295K |