2DCL
Structure of PH1503 protein from Pyrococcus Horikoshii OT3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL26B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL26B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 107.562, 59.647, 66.738 |
| Unit cell angles | 90.00, 122.47, 90.00 |
Refinement procedure
| Resolution | 32.820 - 2.280 |
| R-factor | 0.244 |
| Rwork | 0.244 |
| R-free | 0.29000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1o51 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.500 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.360 |
| High resolution limit [Å] | 2.280 | 2.280 |
| Number of reflections | 15774 | |
| <I/σ(I)> | 16.5 | 2.3 |
| Completeness [%] | 96.9 | 83.9 |
| Redundancy | 3.4 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 4.5 | 295 | 20% PEG 3000, 100mM Acetate, pH 4.5, microbatch, temperature 295.0K |
