1X0T
Crystal structure of ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 42.594, 52.691, 62.672 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.230 - 1.600 |
| R-factor | 0.217 |
| Rwork | 0.217 |
| R-free | 0.24500 |
| Structure solution method | MAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 1.100 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.1) |
| 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 | 0.053 | 0.460 |
| Number of reflections | 23409 | |
| <I/σ(I)> | 23 | 2.6 |
| Completeness [%] | 98.5 | 87.7 |
| Redundancy | 6.9 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | VAPOR DIFFUSION, HANGING DROP |
