6MAX
Crystal structure of Ribonuclease P protein from Thermotoga maritima in complex with purpurin
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-08-10 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9785 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 60.427, 32.730, 64.160 |
| Unit cell angles | 90.00, 113.23, 90.00 |
Refinement procedure
| Resolution | 51.910 - 1.420 |
| R-factor | 0.143 |
| Rwork | 0.141 |
| R-free | 0.18100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nz0 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.069 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 51.910 | 1.440 |
| High resolution limit [Å] | 1.420 | 1.420 |
| Rmerge | 0.055 | 0.394 |
| Number of reflections | 22032 | 1066 |
| <I/σ(I)> | 11.2 | 1.7 |
| Completeness [%] | 99.7 | 97.2 |
| Redundancy | 4.7 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 293 | 100 mM Sodium acetate trihydrate pH 4.8, 200 mM K2SO4, PEG 1000 12% |
