1ORG
The crystal structure of a pheromone binding protein from the cockroach Leucophaea maderae reveals a new mechanism of pheromone binding
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-07-23 |
Detector | MARRESEARCH |
Wavelength(s) | 0.97887 |
Spacegroup name | P 1 |
Unit cell lengths | 43.303, 44.930, 45.562 |
Unit cell angles | 118.13, 93.18, 107.15 |
Refinement procedure
Resolution | 20.000 - 1.700 |
R-factor | 0.18404 |
Rwork | 0.181 |
R-free | 0.18100 * |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.430 * |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.045 | 0.274 * |
Number of reflections | 29653 | |
<I/σ(I)> | 8 | 2.4 |
Completeness [%] | 95.7 * | 94.8 |
Redundancy | 6.0 * | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 8 | 293 | Sulzenbacher, G., (2002) Acta Cryst., D58, 2109. * |