2ERB
AgamOBP1, and odorant binding protein from Anopheles gambiae complexed with PEG
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-08 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.88557 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 30.100, 68.210, 61.480 |
| Unit cell angles | 90.00, 99.77, 90.00 |
Refinement procedure
| Resolution | 30.300 - 1.500 |
| R-factor | 0.172 |
| Rwork | 0.172 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Monomer of model generated from MAD experiments. |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.500 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | CNS |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.540 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.038 | 0.133 |
| Number of reflections | 39190 | |
| <I/σ(I)> | 3.1 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 3.8 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 32% PEG 8000, 250 mM MgCl2, 50 mM Tris HCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
