4CQH
Structure of Infrared Fluorescent Protein IFP2.0
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 | 2013-09-17 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 95.692, 52.912, 66.316 |
| Unit cell angles | 90.00, 91.37, 90.00 |
Refinement procedure
| Resolution | 27.330 - 1.140 |
| R-factor | 0.13825 |
| Rwork | 0.137 |
| R-free | 0.15996 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2o9c |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.963 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.300 | 1.160 |
| High resolution limit [Å] | 1.140 | 1.140 |
| Rmerge | 0.060 | 0.640 |
| Number of reflections | 114179 | |
| <I/σ(I)> | 13.4 | 2.1 |
| Completeness [%] | 99.8 | 99.7 |
| Redundancy | 4 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.6 | 30% PEG 400, 100 MM SODIUM ACETATE PH 4.6 |
