2DVO
Structure of PH1917 protein with the complex of ITP from Pyrococcus horikoshii
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 | IMAGE PLATE |
| Collection date | 2004-02-28 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 78.261, 93.068, 54.051 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.210 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1v7r |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.200 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.055 | |
| Number of reflections | 10176 | |
| <I/σ(I)> | 14 | |
| Completeness [%] | 99.5 | 96.1 |
| Redundancy | 5.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 9.1 | 295 | PEG, Dioxnae, Bicine, pH 9.1, microbatch, temperature 295K |
