2IT2
Structure of PH1069 protein from Pyrococcus horikoshii
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 | 2006-04-06 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 37.428, 53.902, 53.212 |
| Unit cell angles | 104.60, 102.90, 109.30 |
Refinement procedure
| Resolution | 17.550 - 1.500 |
| R-factor | 0.25 |
| Rwork | 0.250 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2drv |
| RMSD bond length | 0.008 |
| 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] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.054 | |
| Number of reflections | 53423 | |
| <I/σ(I)> | 21.9 | |
| Completeness [%] | 100.0 | 99 |
| Redundancy | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 7.5 | 295 | HEPES, KH2PO4, pH 7.5, microbatch, temperature 295K |
