2C0F
Structure of Wind Y53F mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-12-17 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 109.444, 51.719, 100.655 |
| Unit cell angles | 90.00, 112.70, 90.00 |
Refinement procedure
| Resolution | 20.240 - 2.280 |
| R-factor | 0.222 |
| Rwork | 0.219 |
| R-free | 0.28100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ovn |
| RMSD bond length | 0.031 |
| RMSD bond angle | 2.377 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.370 |
| High resolution limit [Å] | 2.280 | 2.280 |
| Rmerge | 0.040 | 0.200 |
| Number of reflections | 22333 | |
| <I/σ(I)> | 10.94 | 3.26 |
| Completeness [%] | 97.6 | 88.2 |
| Redundancy | 1.77 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.8 | PROTEIN: 18.0MG/ML Y53F IN 5MM HEPES PH7.5, 25MM LICL, 0.0025%(V/V) BETA-MERCAPTOETHANOL RESERVOIR: 0.1M MES PH5.8, 50MM LICL, 18%(V/V) PEG 400 CRYO: 0.1M MES PH6.0, 25%(V/V) PEG 400,50MM LICL, pH 5.80 |
