3FE6
Crystal structure of a pheromone binding protein from Apis mellifera with a serendipitous ligand at pH 5.5
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-24 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 82.879, 84.210, 46.831 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.16112 |
| Rwork | 0.159 |
| R-free | 0.19289 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1R5R |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.365 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC (5.4.0077) |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.110 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.079 | 0.448 |
| Number of reflections | 15535 | |
| <I/σ(I)> | 22.9 | 4.3 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7.8 | 7.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 1.7M ammonium sulfate, 0.1M sodium citrate, pH5.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
