4Q2R
Structural Proteomics From Crude Native Rod Outer Segments
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-04-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.07500 |
| Spacegroup name | P 43 |
| Unit cell lengths | 95.976, 95.976, 107.090 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.922 - 1.650 |
| R-factor | 0.22275 |
| Rwork | 0.222 |
| R-free | 0.24575 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3b6r |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.966 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MLPHARE |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.922 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.087 | 0.074 |
| Number of reflections | 116751 | |
| <I/σ(I)> | 45.4 | 2.8 |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 6.2 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 277 | 1.8 M ammonium sulfate, 0.1 M HEPES, 3% PEG 1K, pH 7.5, VAPOR DIFFUSION, temperature 277K |
