3R72
Apis mellifera odorant binding protein 5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-07-27 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.695, 45.239, 70.882 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.130 - 1.150 |
| R-factor | 0.15289 |
| Rwork | 0.152 |
| R-free | 0.17253 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.341 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.130 | 1.210 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.046 | 0.500 |
| Number of reflections | 42573 | |
| <I/σ(I)> | 17.5 | 2.4 |
| Completeness [%] | 99.4 | 97.1 |
| Redundancy | 5.8 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4 | 298 | 20-25% PEG1500, MIB pH 3.7-4, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
