3S0A
Apis mellifera OBP14, native apo-protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-08 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 32.410, 37.990, 86.380 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.190 - 1.150 |
| R-factor | 0.15602 |
| Rwork | 0.155 |
| R-free | 0.17797 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3rzs |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.481 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.100 | 1.180 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.045 | 0.500 |
| Number of reflections | 37980 | |
| <I/σ(I)> | 18.7 | 2.1 |
| Completeness [%] | 98.0 | 86.1 |
| Redundancy | 5.3 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.8 | 293 | 1.8-1.9 M tri-sodium citrate, 25 mM CHES, pH 9.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
