3BFB
Crystal structure of a pheromone binding protein from Apis mellifera in complex with the 9-keto-2(E)-decenoic acid
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 | 2007-09-08 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.099, 84.281, 47.602 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.150 |
| R-factor | 0.20848 |
| Rwork | 0.204 |
| R-free | 0.25223 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1R5R |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.279 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | REFMAC (5.2.0019) |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.300 | 2.270 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmerge | 0.072 | 0.492 |
| Number of reflections | 9124 | |
| <I/σ(I)> | 16.6 | 3.8 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 6.9 | 7.2 |
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 |
