2ZAE
Crystal structure of protein Ph1601p in complex with protein Ph1771p of archaeal ribonuclease P from Pyrococcus horikoshii OT3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | RIGAKU JUPITER 210 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 74.829, 127.070, 51.857 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.640 - 2.210 |
| R-factor | 0.20191 |
| Rwork | 0.199 |
| R-free | 0.25005 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1x0t 1v76 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.397 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.064 | 0.369 |
| Number of reflections | 25221 | |
| <I/σ(I)> | 33.8 | 3.15 |
| Completeness [%] | 98.6 | 89.6 |
| Redundancy | 6 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293.4 | 20% PEG 3350, 0.2M KNO3, 50mM NaCl,50mM Tris-HCl , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.4K |
