1V76
Crystal Structure of Archaeal Ribonuclease P Protein Ph1771p from Pyrococcus horikoshii OT3
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL38B1 |
Synchrotron site | SPring-8 |
Beamline | BL38B1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-10-30 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.97972, 0.90 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 24.133, 56.271, 71.756 |
Unit cell angles | 90.00, 96.80, 90.00 |
Refinement procedure
Resolution | 30.100 - 2.000 |
R-factor | 0.209 |
Rwork | 0.209 |
R-free | 0.25700 |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.096 | 0.240 |
Number of reflections | 25204 | |
<I/σ(I)> | 14.6 | 8.8 |
Completeness [%] | 99.7 | 99.1 |
Redundancy | 3.7 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 1.0M ammonium sulfate, 100mM Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |