2IT3
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 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-04-12 |
| Detector | RIGAKU RAXIS V |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 40.673, 57.951, 167.416 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.24 |
| Rwork | 0.240 |
| R-free | 0.27000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2drv |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.352 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.079 | |
| Number of reflections | 22800 | |
| <I/σ(I)> | 9 | |
| Completeness [%] | 99.7 | 99.7 |
| Redundancy | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 6.6 | 295 | MES, NaCl, pH 6.6, microbatch, temperature 295K |
