6CQC
RNase P protein from Thermotoga maritima in complex with 1-(4-Fluorophenyl)-2-thiourea
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-11-12 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9785 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 56.136, 64.264, 68.121 |
| Unit cell angles | 90.00, 101.63, 90.00 |
Refinement procedure
| Resolution | 46.286 - 1.540 |
| R-factor | 0.1811 |
| Rwork | 0.180 |
| R-free | 0.19900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nz0 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.703 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.290 | 1.570 |
| High resolution limit [Å] | 1.540 | 1.540 |
| Rmerge | 0.044 | 0.237 |
| Rmeas | 0.053 | 0.287 |
| Rpim | 0.029 | 0.195 |
| Number of reflections | 67977 | 2724 |
| <I/σ(I)> | 19.5 | 3.7 |
| Completeness [%] | 96.9 | 78.5 |
| Redundancy | 3.2 | 2.9 |
| CC(1/2) | 0.993 | 0.915 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 292 | P protein from T. maritima in 50 mM Tris-HCl pH 7.5, 0.2 mM EDTA was crystallized at 3 mg/mL in 12% PEG-1000, 100 mm sodium acetate pH 4.8 and 200 mM potassium sulfate |






