2D16
Crystal Structure of PH1918 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 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-07-20 |
| Detector | RIGAKU |
| Wavelength(s) | 0.9 |
| Spacegroup name | P 3 |
| Unit cell lengths | 66.120, 66.120, 125.072 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.700 - 1.650 |
| R-factor | 0.185 |
| Rwork | 0.185 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vgg |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.400 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.710 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.066 | |
| Number of reflections | 73383 | |
| <I/σ(I)> | 7.1 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6.3 | 295 | MES-NaOH, PEG 4000, pH 6.3, microbatch, temperature 295.0K |
