3SW1
Structure of a full-length bacterial LOV protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-06 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.8726 |
| Spacegroup name | P 61 |
| Unit cell lengths | 55.067, 55.067, 221.993 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.626 - 2.630 |
| R-factor | 0.2118 |
| Rwork | 0.210 |
| R-free | 0.23940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1n9l |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.316 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((phenix.refine: 1.7_632)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.500 | 2.680 |
| High resolution limit [Å] | 2.630 | 2.630 |
| Rmerge | 0.064 | 0.461 |
| Number of reflections | 11307 | |
| <I/σ(I)> | 15.4 | 2.6 |
| Completeness [%] | 99.8 | 95.9 |
| Redundancy | 6.1 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 7.5 | 292.15 | 100 mM Tris, 8-18% w/v PEG3350, pH 7.5, VAPOR DIFFUSION, temperature 292.15K |
