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 |