5JOR
Crystal structure of unbound anti-glycan antibody Fab14.22 at 2.2 A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 293 |
| Detector technology | PIXEL |
| Collection date | 2014-06-15 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.03321 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 120.613, 75.992, 122.946 |
| Unit cell angles | 90.00, 100.58, 90.00 |
Refinement procedure
| Resolution | 49.733 - 2.206 |
| R-factor | 0.2068 |
| Rwork | 0.205 |
| R-free | 0.23690 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qgc |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.520 |
| Data reduction software | HKL-2000 (v706e) |
| Data scaling software | HKL-2000 (v706e) |
| Phasing software | PHASER (2.5.6) |
| Refinement software | PHENIX ((1.10_2155: 000)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.740 | 2.231 |
| High resolution limit [Å] | 2.206 | 2.206 |
| Rmerge | 0.680 | |
| Number of reflections | 109255 | |
| <I/σ(I)> | 6.1 | 1.6 |
| Completeness [%] | 99.4 | 95.3 |
| Redundancy | 3.6 | 3.1 |
| CC(1/2) | 0.902 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 1:1 (v/v) protein/reservoir drop equilibrated against 3.6M ammonium sulfate, with 10% PEG400 and 10%MPD, in 1M of HEPES (pH 7.5) reservoir solution |
