3BFH
Crystal structure of a pheromone binding protein from Apis mellifera in complex with hexadecanoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-04-29 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.934 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 80.260, 84.348, 47.666 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 2.000 |
| R-factor | 0.17609 |
| Rwork | 0.173 |
| R-free | 0.21032 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1R5R |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.410 |
| 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] | 58.720 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.062 | 0.459 |
| Number of reflections | 11157 | |
| <I/σ(I)> | 15.2 | 3.8 |
| Completeness [%] | 99.1 | 99.5 |
| Redundancy | 5 | 5.1 |
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 |
