2C0G
Structure of PDI-related Chaperone, Wind mutant-Y53S
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 | 108.476, 50.557, 98.900 |
| Unit cell angles | 90.00, 112.06, 90.00 |
Refinement procedure
| Resolution | 25.000 - 1.750 |
| R-factor | 0.222 |
| Rwork | 0.219 |
| R-free | 0.26800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ovn |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.784 |
| 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] | 25.000 | 1.850 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.040 | 0.260 |
| Number of reflections | 47523 | |
| <I/σ(I)> | 19.32 | 3.96 |
| Completeness [%] | 99.1 | 95.9 |
| Redundancy | 3.86 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | PROTEIN: 10.0MG/ML Y53S IN 5MM HEPES PH7.5, 25MM NACL, 0.0025%(V/V) BETA-MERCAPTOETHANOL RESERVOIR: 0.1M MES PH6.0, 50MM NACL, 18%(V/V) PEG 400 5% GLYCEROL CRYO: 0.1M MES PH6.0, 25%(V/V) PEG 400, 10%(V/V)GLYCEROL,50MM NACL, pH 6.00 |
